{"title":"Proteins","description":"Books on the subject of Proteins","products":[{"product_id":"protein-condensation-kinetic-pathways-to-crystallization-and-disease-hardback-9780521851213","title":"Protein Condensation; Kinetic Pathways to Crystallization and Disease (Hardback) 9780521851213","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProtein Condensation\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eKinetic Pathways to Crystallization and Disease\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cem\u003eExplains for researchers the rapidly evolving field of protein condensation and the relation to disease.\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eJames D. Gunton (Author), Andrey Shiryayev (Author), Daniel L. Pagan (Author)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780521851213, Cambridge University Press\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 20 September 2007\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e376 pages\u003cbr\u003e25 x 17.5 x 2 cm, 0.92 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e'… the text covers just about anything a researcher would need to know of the many research areas of protein crystallisation. From statistical tests to theoretical models and mathematics, Gunton et al. appear to include the lot.' Journal of Biological Education\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThe quest to understand the condensation of proteins from solutions is a rapidly evolving field. The purpose of this book is to bring to an interdisciplinary audience the state-of-the-art in current research. The first part of the book deals with issues related to the production of high quality protein crystals from solution. Since protein function is determined by structure, high quality protein crystals must be grown in order to determine their structure by X-ray crystallography. The book also discusses diseases that occur due to undesired protein condensation, an increasingly important subject. Examples include sickle cell anemia, cataracts and Alzheimer's disease. Current experimental and theoretical work on these diseases is discussed, which seeks understanding at a fundamental, molecular level, to prevent the undesired condensation from occurring. The book, containing color plate sections, is suitable for graduate students and academic researchers in physics, chemistry, structural biology, protein crystallography and medicine.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePreface\u003cbr\u003e 1. Introduction\u003cbr\u003e 2. Globular protein structure\u003cbr\u003e 3. Experimental methods\u003cbr\u003e 4. Thermodynamics and statistical mechanics\u003cbr\u003e 5. Protein-protein interactions\u003cbr\u003e 6. Theoretical studies of equilibrium\u003cbr\u003e 7. Nucleation theory\u003cbr\u003e 8. Experimental studies of nucleation\u003cbr\u003e 9. Lysozyme\u003cbr\u003e 10. Some other globular proteins\u003cbr\u003e 11. Membrane proteins\u003cbr\u003e 12. Crystallins and cataracts\u003cbr\u003e 13. Sickle hemoglobin and sickle cell anemia\u003cbr\u003e 14, Alzheimer's disease\u003cbr\u003e Index.\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Cambridge University Press","offers":[{"title":"Default Title","offer_id":46005918859544,"sku":"9780521851213","price":98.39,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780521851213i_1c296b38-9086-4d63-95b7-0466a8629c61.jpg?v=1691368818"},{"product_id":"guide-to-protein-purification-paperback-9780123749789","title":"Guide to Protein Purification (Paperback \/ softback) 9780123749789","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eGuide to Protein Purification\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cp\u003eAn essential reference for any researcher involved in protein purification, this volume is a comprehensive collection of methods necessary for purifying, characterizing, and handling proteins and enzymes\u003c\/p\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRichard R Burgess (Edited by), Murray P. Deutscher (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123749789\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePaperback \/ softback, published 1 December 2009\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e912 pages\u003cbr\u003e22.9 x 15.1 x 5.5 cm, 1.19 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\u003ci\u003eGuide to Protein Purification, Second Edition\u003c\/i\u003e provides a complete update to existing methods in the field, reflecting the enormous advances made in the last two decades. In particular, proteomics, mass spectrometry, and DNA technology have revolutionized the field since the first edition’s publication but through all of the advancements, the purification of proteins is still an indispensable first step in understanding their function. This volume examines the most reliable, robust methods for researchers in biochemistry, molecular and cell biology, genetics, pharmacology, biotechnology and sets a standard for best practices in the field. It relates how these traditional and new cutting-edge methods connect to the explosive advancements in the field. This \"Guide to\" gives imminently practical advice in order to avoid costly mistakes in choosing a method and brings in perspective from the premier researchers while it presents a comprehensive overview of the field today. \u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e1. Why Purify Enzymes? 2. Strategies and Considerations for Protein Purifications (Linn) 3. Bioinformatics in Planning a Protein Purification (Burgess) 4. Preparing a Protein Purification Summary Table (Burgess) 5. Setting up a Laboratory (Deutscher) 6. Buffers: Principle and Practice (Blanchard) 7. Measurement of Enzyme Activity (Harris) 8. Quantitation of Protein (Bailey and Noble) 9. Maintaining Protein Stability (Deutscher) 10. Strategy for Choosing and Expression System (Brondyk) 11. Bacterial Expression Systems (Collart) 12. Yeast Expression Systems (Cregg) 13. Baculovirus-Insect Cell Expression Systems (Jarvis) 14. Mammalian Expression Systems (Geisse and Knopf) 15. Expression of Tagged Proteins (Melhorta) 16. Re-folding of Solubilized Inclusion Body Proetin (Burgess) 17. Preparation of Biological Extract (Grabski)\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Science: general issues [\u003ca title=\"See our other books on Science: general issues\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Science:%20general%20issues%20%5BPD%5D%22\"\u003ePD\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46648491770136,"sku":"9780123749789","price":64.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123749789.jpg?v=1695013952"},{"product_id":"protein-biochemistry-and-proteomics-paperback-9780120885459","title":"Protein Biochemistry and Proteomics (Paperback \/ softback) 9780120885459","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProtein Biochemistry and Proteomics\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eNot a typical laboratory book, but an innovative, tactical, guide to avoid frustration in the biochemical lab!\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eHubert Rehm (Author)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780120885459, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePaperback \/ softback, published 24 March 2006\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e256 pages\u003cbr\u003e26 x 18.3 x 1.7 cm, 0.59 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e“It will provide you with the necessary tools for success…if you are a protein biochemist, what are you waiting for? Grab the Experimenter and get experimenting!? \u003cb\u003e--Weanée Kimblewood for LAB TIMES (2006)\u003c\/b\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eHubert Rehm's \u003ci\u003eProtein Biochemistry and Proteomics\u003c\/i\u003e is more than a laboratory manual; it is a strategic guide that provides the reader with tips and tricks for more successful lab experiments. Using a conversational yet professional tone, Rehm provides an overview of a variety of methods in protein biochemistry\/proteomics. He provides short and precise summaries of routine procedures as well as listings of the advantages and disadvantages of alternative methods. Readers will immediately sense that the author if very familiar with the challenges, and frustration of the daily lab routine. Never before has such an honest, tactical guide been available for those conducting lab experiments within the field of biochemistry.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eThe Concept of the Experimenter\u003cbr\u003ePreface to the 4th edition\u003cbr\u003eAcknowledgments\u003cbr\u003eAbbreviations\u003cbr\u003e1. The Daily Bread\u003cbr\u003e2. Ligand Binding\u003cbr\u003e3. Solubilization of membrane proteins\u003cbr\u003e4. Protein detection via functional measurements\u003cbr\u003e5. Cleaning and Purifying\u003cbr\u003e6. Antibodies\u003cbr\u003e7. Proteomics\u003cbr\u003e8. Subunits\u003cbr\u003e9. Glycoproteins\u003cbr\u003e10. Treasure Island\u003cbr\u003e11. Desert Planet\u003cbr\u003e12. Jaws\u003cbr\u003eLast Things\u003cbr\u003eIndex\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], DNA \u0026amp; Genome [\u003ca title=\"See our other books on DNA \u0026amp; Genome\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22DNA%20\u0026amp;%20Genome%20%5BPSAK1%5D%22\"\u003ePSAK1\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46648846680344,"sku":"9780120885459","price":37.29,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780120885459_cedbc874-381b-4718-b087-222b912635ce.jpg?v=1695006620"},{"product_id":"peptides-synthesis-structures-and-applications-hardback-9780123109200","title":"Peptides; Synthesis, Structures, and Applications (Hardback) 9780123109200","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003ePeptides\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eSynthesis, Structures, and Applications\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eBernd Gutte (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123109200, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 24 October 1995\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e511 pages\u003cbr\u003e22.9 x 15.1 x 3 cm, 0.87 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eIn recent years, research has shown the importance of peptides in neuroscience, immunology, and cell biology. Active research programs worldwide are now engaged in developing peptide-based drugs and vaccines using modification of natural peptides and proteins, design of artificial peptides and peptide mimetics, and screening of peptide and phage libraries.\u003c\/p\u003e  \u003cp\u003eIn this comprehensive book, the authors discuss peptide synthesis and application within the context of their increasing importance to the pharmaceutical industry. \u003ci\u003ePeptides: Synthesis, Structures, and Applications\u003c\/i\u003e explores the broad growth of information in modern peptide synthetic methods and the structure-activity relationships of synthetic polypeptides.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eThe History of Peptide Chemistry Amide Formation, Deprotection, And Disulfide Formation in Peptide Synthesis Solid Phase Peptide Synthesis A-Helix Formation By Peptides in Water Peptide Conformation: Stability and Dynamics Structure-Function Studies of Peptide Hormones: An Overview Neuropeptides: Peptides and Nonpeptide Analogs Reversible Inhibitors of Serine Proteinases, Naturallly Occurring Miniproteins, Semisynthetic Variants, Recombinant Homologues and Synthetic Peptides Design of Polypeptides Chemical Combinatorial Libraries: Current Capabilities and Future Possibilities Epitope Mapping with Peptides Active Immunization Using Synthetic Peptides \u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Pharmacology [\u003ca title=\"See our other books on Pharmacology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Pharmacology%20%5BMMG%5D%22\"\u003eMMG\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649083068696,"sku":"9780123109200","price":42.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123109200_64704dcd-dc5b-48e8-874a-ca9584821946.jpg?v=1695006725"},{"product_id":"copper-containing-molecules-hardback-9780120342600","title":"Copper-Containing Molecules (Hardback) 9780120342600","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eCopper-Containing Molecules\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eJoan S. Valentine (Edited by), Edith B. Gralla (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780120342600, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 1 November 2002\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e493 pages\u003cbr\u003e22.9 x 15.1 x 3 cm, 0.79 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003ePRAISE FOR THE SERIES\u003cbr\u003e\"The authority, originality, and editing of the reviews are first class.\" \u003cb\u003e--NATURE \u003cbr\u003e\u003c\/b\u003e\u003cbr\u003e\"The Advances in Protein Chemistry series has been a major factor in the education of protein chemists.\" \u003cb\u003e--JOURNAL OF THE AMERICAN CHEMICAL SOCIETY\u003c\/b\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eA wide range of researchers are currently investigating different properties and applications for copper-containing proteins. Biochemists researching metal metabolism in organisms ranging from bacteria to plants to animals are working in a completely different area of discovery than scientists studying the transportation and regulation of minerals and small molecule nutrients. They are both working with copper-containing proteins, but in very different ways and with differing anticipated outcomes.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Chemistry [\u003ca title=\"See our other books on Chemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Chemistry%20%5BPN%5D%22\"\u003ePN\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649175245080,"sku":"9780120342600","price":77.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780120342600_47a4e38e-654f-4c0a-bdf0-fb1ddcf05e95.jpg?v=1695006578"},{"product_id":"novel-cofactors-hardback-9780120342587","title":"Novel Cofactors (Hardback) 9780120342587","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eNovel Cofactors\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eJudith P. Klinman (Volume editor), Joanne E. Dove (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780120342587, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 16 October 2001\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e474 pages\u003cbr\u003e22.9 x 15.2 x 2.9 cm, 0.81 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003ePraise for the Series:\u003cbr\u003e\"The authority, originality, and editing of the reviews are first class.\" \u003cb\u003e--NATURE\u003cbr\u003e\u003c\/b\u003e\u003cbr\u003e\"The Advances in Protein Chemistry series has been a major factor in the education of protein chemists.\" \u003cb\u003e--JOURNAL OF THE AMERICAN CHEMICAL SOCIETY\u003c\/b\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eA cofactor is a component part of many enzymes and functions by uniting with another molecule in order to become active. \u003cbr\u003eThe use of cofactors to supplement the native amino acids of a protein is essential to maintain the chemical capabilities necessary for organisms to survive. This volume focuses on the significant advances of the past decade in identifying and describing new cofactors--either small molecules or those derived posttranslationally.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePreface.\u003cbr\u003eRadical Mechanisms of S-Adenosylmethionine-Dependent Enzymes,\u003cbr\u003e\u003ci\u003eP.A. Frey and S.J. Booker\u003c\/i\u003e.\u003cbr\u003eMolybdopterin from Molybdenum and Tungsten Enzymes,\u003cbr\u003e\u003ci\u003eH. Schindelin, C. Kisker, and K.V. Rajagopalan\u003c\/i\u003e.\u003cbr\u003ePyrroloquinoline Quinone (PQQ) from Methanol Dehydrogenase and Tryptophan Tryptophylquinone (TTQ) from Methylamine Dehydrogenase,\u003cbr\u003e\u003ci\u003eV.L. Davidson\u003c\/i\u003e.\u003cbr\u003eTrihydroxyphenylalanine Quinone (TPQ) from Copper Amine Oxidases and Lysyl Tyrosylquinone (LTQ) from Lysyl Oxidase,\u003cbr\u003e\u003ci\u003eJ.E. Dove and J.P. Klinman\u003c\/i\u003e.\u003cbr\u003eMethylidene-Imidazolone (MIO) from Histidine and Phenylalanine Ammonia-Lyase,\u003cbr\u003e\u003ci\u003eB. Langer, M. Langer, and J. Retey\u003c\/i\u003e.\u003cbr\u003eStructural, Redox, and Mechanistic Parameters for Cysteine-Sulfenic Acid Function in Catalysis and Regulation,\u003cbr\u003e\u003ci\u003eA. Claiborne, T.C. Mallett, J.I. Yeh, J. Luba, and D. Parsonage\u003c\/i\u003e.\u003cbr\u003eStable Glycyl Radical from Pyruvate Formate-Lyase and Ribonucleotide Reductase (III),\u003cbr\u003e\u003ci\u003eJ. Knappe and A.F. Volker Wagner\u003c\/i\u003e.\u003cbr\u003eTyrosyl Radical Cofactors,\u003cbr\u003e\u003ci\u003eR.P. Pesavento and W.A. van der Donk\u003c\/i\u003e.\u003cbr\u003ePosttranslationally Modified Tyrosines from Galactose Oxidase and Cytochrome c Oxidase,\u003cbr\u003e\u003ci\u003eM.S. Rogers and D.M. Dooley\u003c\/i\u003e.\u003cbr\u003eAuthor Index.\u003cbr\u003eSubject Index.\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Enzymology [\u003ca title=\"See our other books on Enzymology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Enzymology%20%5BPSBZ%5D%22\"\u003ePSBZ\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649176817944,"sku":"9780120342587","price":114.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780120342587.jpg?v=1694098456"},{"product_id":"peptide-solvation-and-h-bonds-hardback-9780120342723","title":"Peptide Solvation and H-bonds (Hardback) 9780120342723","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003ePeptide Solvation and H-bonds\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eNew Directions in the Study of Peptide H-bonds and Peptide Solvation\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRobert Baldwin (Volume editor), David James Baker (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780120342723, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 15 March 2006\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e312 pages, Illustrated\u003cbr\u003e22.9 x 15.1 x 2.3 cm, 0.63 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003ePRAISE FOR THE SERIES: \u003cbr\u003e\u003cbr\u003e\"The authority, originality, and editing of the reviews are first class.\" \u003cb\u003e--NATURE\u003cbr\u003e\u003c\/b\u003e\u003cbr\u003e\"The Advances in Protein Chemistry series has been a major factor in the education of protein chemists.\" \u003cb\u003e--JOURNAL OF THE AMERICAN CHEMICAL SOCIETY\u003c\/b\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eVolume 72, \u003ci\u003ePeptide Solvation and H-bonds\u003c\/i\u003e, addresses the role of peptide backbone solvation in the energetics of protein folding. Particular attention is focused on modeling and computation. This volume will be of particular interest to biophysicists and structural biologists.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePreface: New Directions in the Study of Peptide H-bonds and Peptide Solvation\u003cbr\u003e Potential Functions for Hydrogen Bonds in Protein Structure Prediction and Design\u003cbr\u003e Backbone-Backbone H-Bonds Make Context Dependent Contributions to Protein Folding Kinetics and Thermodynamics: Lessons from Amide-to-Ester Mutations\u003cbr\u003e Modeling Polarization in Proteins and Protein-Ligand Complexes: Methods and Preliminary Results\u003cbr\u003e Hydrogen Bonds in Molecular Mechanics Force Fields\u003cbr\u003e Resonance Character of Hydrogen-Bonding Interactions in Water and Other H-Bonded Species\u003cbr\u003e How Hydrogen Bonds Shape Membrane Protein Structure\u003cbr\u003e Peptide and Protein Folding and Conformational Equilibria: Theoretical Treatment of Electrostatics and Hydrogen Bonding with Implicit Solvent Models\u003cbr\u003e Thermodynamics of \u0026amp;alpha\u003cbr\u003e-Helix Formation\u003cbr\u003e The Importance of  Cooperative Interactions and A Solid State Paradigm to Proteins – What Peptide Chemists Can Learn from Molecular Crystals\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649177702680,"sku":"9780120342723","price":77.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780120342723_bba633e3-5be0-4768-898f-511847124556.jpg?v=1695006563"},{"product_id":"protein-lipidation-hardback-9780121227227","title":"Protein Lipidation (Hardback) 9780121227227","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProtein Lipidation\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eFuyuhiko Tamanoi (Volume editor), David S. Sigman (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780121227227, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 19 October 2000\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e322 pages\u003cbr\u003e22.9 x 15.2 x 2.4 cm, 0.6 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThis is the first compilation of protein lipidation enzymes. This volume summarizes recent dramatic developments regarding enzymes responsible for protein lipidation, a process critical for a number of physiological functions, including cell proliferation and morphology. Inhibitors of protein lipidation have recently been shown to be useful as anticancer drugs. Enzymatic mechanisms, mutational analysis, and structural studies are presented.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eMechanism of Catalysis by Protein Farnesyltransferase\u003cbr\u003eStructure of Protein Farnesyltransferase\u003cbr\u003eMutational Analyses of Protein Farnesyltransferase\u003cbr\u003eFarnesyltransferase Inhibitors\u003cbr\u003eProtein Geranylgeranyltransferase Type I\u003cbr\u003eBiochemistry of Rab Geranylgeranyltransferase\u003cbr\u003ePostisoprenylation Protein Processing: CXXX (CaaX) Endoproteases and Isoprenylcysteine Carboxyl Methyltransferase\u003cbr\u003eReversible Modification of Proteins with Thioester-Linked Fatty Acids\u003cbr\u003eBiology and Enzymology of Protein N-Myristoylation\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Enzymology [\u003ca title=\"See our other books on Enzymology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Enzymology%20%5BPSBZ%5D%22\"\u003ePSBZ\u003c\/a\u003e], Lipids [\u003ca title=\"See our other books on Lipids\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Lipids%20%5BPSBH%5D%22\"\u003ePSBH\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649179963672,"sku":"9780121227227","price":71.39,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780121227227.jpg?v=1694098474"},{"product_id":"proteins-in-eukaryotic-transcription-hardback-9780120342679","title":"Proteins in Eukaryotic Transcription (Hardback) 9780120342679","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProteins in Eukaryotic Transcription\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThis volume covers structure and function of all major elements associated with transcription.\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRon C Conaway (Volume editor), Joan W. Conaway (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780120342679, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 19 March 2004\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e280 pages\u003cbr\u003e22.9 x 15.1 x 2.2 cm, 0.65 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eProtein Transcription is a key element of cellular and organ regulation. \u003ci\u003eProteins in Eukaryotic Transcription\u003c\/i\u003e covers structure and function of all major elements associated with transcription.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eStructure and function of RNA Polymerase II\u003cbr\u003e the mediator complex\u003cbr\u003e structure and function of the TFIID complex\u003cbr\u003e the tetratricopeptide repeats of Tfc4\u003cbr\u003e mechanism of RNA polymerase I transcription\u003cbr\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Genetics [\u003ca title=\"See our other books on Genetics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Genetics%20%5Bnon-medical%5D%20%5BPSAK%5D%22\"\u003enon-medical PSAK\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649180782872,"sku":"9780120342679","price":102.89,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780120342679_c4796565-d7bf-419b-b5e7-68157ca8d1fb.jpg?v=1695006572"},{"product_id":"protein-engineering-and-design-hardback-9780121596408","title":"Protein Engineering and Design (Hardback) 9780121596408","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProtein Engineering and Design\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003ePaul R. Carey (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780121596408, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 21 June 1996\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e361 pages\u003cbr\u003e22.9 x 15.1 x 2.5 cm, 0.68 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThe design and production of novel peptides and proteins occupy pivotal positions in science and technology and will continue to do so in the 21st century. \u003ci\u003eProtein Engineering and Design\u003c\/i\u003e outlines the rapid advances in computer-based modeling, protein engineering, and methods needed for protein and peptide preparation and characterization. This indispensable reference lays the groundwork for understanding this multidisciplinary activity while providing an introduction for researchers and students to the field of protein design.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cb\u003ePrediction:\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eM.H. Hecht\u003c\/i\u003e, Strategies for the Design of Novel Proteins.\u003cbr\u003e\u003ci\u003eJ. Novotny\u003c\/i\u003e, Computer Methods in Protein Modeling: An Overview.\u003cbr\u003e\u003cb\u003eProduction:\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eJ.R. Rose and C.S. Craik\u003c\/i\u003e, The Art of Expression: Sites and Strategies for Heterologous Expression.\u003cbr\u003e\u003ci\u003eV.L. MacKay and T. Kelleher\u003c\/i\u003e, Methods for Expressing Recombinant Proteins in Yeast.\u003cbr\u003e\u003ci\u003eT. Vernet and R. Brousseau, In Vitro\u003c\/i\u003e Mutagenesis.\u003cbr\u003e\u003cb\u003eCharacterization:\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eG.M. Clore and A.M. Gronenborn\u003c\/i\u003e, Determination of Structures of Larger Proteins in Solution by Three- and Four-Dimensional Heteronuclear Magnetic Resonance Spectroscopy.\u003cbr\u003e\u003ci\u003eD. Ringe and G.A. Petsko\u003c\/i\u003e, A Consumer's Guide to Protein Crystallography.\u003cbr\u003e\u003ci\u003eP.R. Carey and W. Surewicz\u003c\/i\u003e, Spectroscopic and Calorimetric Methods for Characterizing Proteins and Peptides.\u003cbr\u003e\u003cb\u003eApplications:\u003c\/b\u003e\u003cbr\u003e\u003ci\u003eA. Nathan and J. Kohn\u003c\/i\u003e, The Design of Polymeric Biomaterials from Natural Alpha-L-Amino Acids.\u003cbr\u003e\u003ci\u003eK.E. McLane, S.J. M.Dunn, A.A. Manfredi, B.M. Conti-Tronconi, and M.A. Raftery\u003c\/i\u003e, The Nicotinic Acetylcholine Receptor as a Model for a Superfamily of Ligand-Gated Ion Channel Proteins\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Medical bioinformatics [\u003ca title=\"See our other books on Medical bioinformatics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Medical%20bioinformatics%20%5BMBF%5D%22\"\u003eMBF\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649186877720,"sku":"9780121596408","price":99.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780121596408_8b3c68d2-839e-4c74-9054-68548c96b115.jpg?v=1695006644"},{"product_id":"protein-targeting-transport-and-translocation-hardback-9780122007316","title":"Protein Targeting, Transport, and Translocation (Hardback) 9780122007316","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProtein Targeting, Transport, and Translocation\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThe most comprehensive and definitive work on Protein Targeting, Transport and Translocation!\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRoss Dalbey (Edited by), Gunnar von Heijne (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780122007316, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 9 April 2002\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e336 pages\u003cbr\u003e22.9 x 15.1 x 2.4 cm, 0.87 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\"...Dalbey et al. have summed up what has happened so far in a rapidly moving field of modern cellular biochemistry.\" \u003cb\u003e--EUROPEAN JOURNAL OF CHEMICAL BIOLOGY, 2003\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\"Overall this book provides good summaries of what we know about how proteins are moved between intracellular compartments and how we have studied this problem. Students or anyone wanting to know more about protein trafficking, particularly protein translocation across membranes, will find it a useful guide.\" \u003cb\u003e--CELL, 2002\u003c\/b\u003e\u003c\/p\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003ci\u003eProtein Targeting, Transport, and Translocation\u003c\/i\u003e presents an in-depth overview on the topic of protein synthesis, covering all areas of protein science, including protein targeting, secretion, folding, assembly, structure, localization, quality control, degradation, and antigen presentation. Chapters also include sections on the history of the field as well as summary panels for quick reference. Numerous color illustrations complement the presentation of material. This book is an essential reference for anyone in biochemistry and protein science, as well as an excellent textbook for advanced students in these and related fields.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eMethods in Protein Targeting, Translocation and Transport\u003cbr\u003eTargeting Sequences\u003cbr\u003eProtein Export in Bacteria\u003cbr\u003eProtein Sorting at the Membrane of the Endoplasmic Reticulum\u003cbr\u003eMembrane Protein Insertion into Bacteial Membranes and Endoplasmic Reticulum\u003cbr\u003eDisulfide Bond Formation in Prokaryotes and Eukaryotes\u003cbr\u003eThe Unfolded Protein Response\u003cbr\u003eProtein Quality Control in the Export Pathway: The Endoplasmic Reticulum and its Cytoplasmic Proteasome Connection\u003cbr\u003eTranslocation of Proteins into Mitochondria\u003cbr\u003eThe Import and Sorting of Protein into Chloroplasts\u003cbr\u003eImport of Proteins into Peroxisomes\u003cbr\u003eNucleocytoplasmic Transport\u003cbr\u003eProtein Transport to the Yeast Vacuole\u003cbr\u003eThe Secretory Pathway\u003cbr\u003eVesicular Transport\u003cbr\u003eConclusion\/Perspective\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649190220056,"sku":"9780122007316","price":53.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780122007316_5e454dad-2217-42ed-b015-8dc6462a33cf.jpg?v=1695006716"},{"product_id":"molecular-design-and-modeling-concepts-and-applications-part-a-proteins-peptides-and-enzymes-hardback-9780121821036","title":"Molecular Design and Modeling: Concepts and Applications, Part A: Proteins, Peptides, and Enzymes (Hardback) 9780121821036","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eMolecular Design and Modeling: Concepts and Applications, Part A: Proteins, Peptides, and Enzymes\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eJohn N. Abelson (Editor-in-chief), Melvin I. Simon (Editor-in-chief), John J. Langone (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780121821036, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 2 December 1991\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e824 pages\u003cbr\u003e22.9 x 15.1 x 4.1 cm, 1.27 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003ePraise for the Series\"The Methods in Enzymology series represents the gold-standard.\" \u003cb\u003e--NEUROSCIENCE\u003c\/b\u003e\"Incomparably useful.\" \u003cb\u003e--ANALYTICAL BIOCHEMISTRY\u003c\/b\u003e\"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page.\" \u003cb\u003e--BIO\/TECHNOLOGY\u003c\/b\u003e\"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection.\"\u003cb\u003e --CHEMISTRY IN INDUSTRY\u003c\/b\u003e\"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced.\" \u003cb\u003e--AMERICAN SOCIETY OF MICROBIOLOGY NEWS\u003c\/b\u003e\"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work.\" \u003cb\u003e--ENZYMOLOGIA\u003c\/b\u003e\"A series that has established itself as a definitive reference for biochemists.\" \u003cb\u003e--JOURNAL OF CHROMATOGRAPHY\u003c\/b\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eComputer-based design and modeling, computational approaches, and instrumental methods for elucidating molecular mechanisms of protein folding and ligand-acceptor interactions are included in Volumes 202 and 203, as are genetic and chemical methods for the production of functional molecules including antibodies and antigens, enzymes, receptors, nucleic acids and polysaccharides, and drugs.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cb\u003eProteins and Peptides: Principles and Methods: Protein Folding, Stability, and Function:\u003c\/b\u003e\u003ci\u003eN.M. Allewell and H. Oberoi\u003c\/i\u003e, Electrostatic Effects in Protein Folding, Stability, and Function.\u003ci\u003eC. Lawrence and S. Bryant\u003c\/i\u003e, Hydrophobic Potentials from Statistical Analysis of Protein Structures.\u003ci\u003eK. Nishikawa and T. Noguchi\u003c\/i\u003e, Predicting Protein Secondary Structure Based on Amino Acid Sequence.\u003ci\u003eT. Niermann and K. Kirschner\u003c\/i\u003e, Use of Homologous Sequences to Improve Protein Secondary Structure Prediction.\u003ci\u003eB.L. Sibanda and J.M. Thornton\u003c\/i\u003e, Conformation of ~gb-Hairpins in Protein Structures: Classification and Diversity in Homologous Structures.\u003ci\u003eA. Matouschek and A.R. Fersht\u003c\/i\u003e, Protein Engineering in the Analysis of Protein Folding Pathways and Stability.\u003ci\u003eP.A. ~Jennings, S.M. Saalau-Bethell, B.E. Finn, X. Chen, and C.R. Matthews\u003c\/i\u003e, Mutational Analysis of Protein Folding Mechanisms.\u003cb\u003eDesign and Modeling:\u003c\/b\u003e\u003ci\u003eR.A. Lewis\u003c\/i\u003e, Clefts and Binding Sites in Protein Receptors.\u003ci\u003eN. Summers and M. Karplus\u003c\/i\u003e, Modeling of Side Chains, Loops, and Insertions.\u003ci\u003eL.H. Holley and M. Karplus\u003c\/i\u003e, Neural Networks.\u003ci\u003eV.E. Reyes, R.A. Lew, S. Lu, and R.E. Humphreys\u003c\/i\u003e, Prediction of ~ga Helices and T-Cell-Presented Sequences in Proteins with Algorithms Based on Strip-of-Helix Hydrophobicity Index.\u003ci\u003eJ. Greer\u003c\/i\u003e, Comparative Modeling of Homologous Proteins.\u003ci\u003eB.I. Cohen, S.R. Presnell, and F.E. Cohen\u003c\/i\u003e, Pattern-Based Approaches to Protein Structure Prediction.\u003ci\u003eJ. de Vlieg and W.F. van Gunsteren\u003c\/i\u003e, Combined Procedures of Distance Geometry and Molecular Dynamics ~for Determining Protein Structure from NMR Data.\u003ci\u003eJ. Ellman, S. Anthony-Cahill, C.J. Noren, and P.G. Schultz\u003c\/i\u003e, Biosynthetic Method for Introducing Unnatural Amino Acids Site Specifically into Proteins.\u003ci\u003eM. Matsumura and B.W. Matthews\u003c\/i\u003e, Stabilization of Functional Proteins by Introduction of Multiple Disulfide Bonds.\u003ci\u003eC.A. Hutchison III, R. Swanstrom, and D. Loeb\u003c\/i\u003e, Complete Mutagenesis of Protein Coding Domains.\u003ci\u003eJ.A. Wells\u003c\/i\u003e, Systemic Mutational Analysis of Protein-Protein Interfaces.\u003ci\u003eP.E. Smith, F. Al-Obeidi, and B.M. Pettitt\u003c\/i\u003e, Design of Conformationally Constrained Peptides.\u003ci\u003eW.M. Bryan\u003c\/i\u003e, Design of Minimum Active Fragments of Biologically Active Peptides.\u003ci\u003eA.D. MacKerell, Jr. \u003c\/i\u003e, Molecular Modeling and Dynamics of Biologically Active Peptides: Application~to Neuropeptide Y. \u003cb\u003eEnzymes:\u003c\/b\u003e\u003ci\u003eM.E. Davis, J.D. Madura, J. Sines, B.A. Luty, S.A. Allison and J.A. McCammon\u003c\/i\u003e, Diffusion-Controlled Enzymatic Reactions.\u003ci\u003eT.P. Straatsma and J.A. McCammon\u003c\/i\u003e, Theoretical Calculations of Relative Affinities of Binding.\u003ci\u003eC. Hansch and T.E. Klein\u003c\/i\u003e, QSAR and Molecular Graphics in Evaluation of Enzyme-Ligand Interactions.\u003ci\u003eA.J. Leo\u003c\/i\u003e, Hydrophobic Parameter: Measurement and Calculation.\u003ci\u003eC.-H. Wong, G.-J. Shen, R.L. Pederson, Y.F. Wang, and W.J. Hennen\u003c\/i\u003e, Enzymatic Catalysis in Organic Synthesis.\u003ci\u003eG. Alvaro and A.J. Russell\u003c\/i\u003e, Modification of Enzyme Catalysis by Engineering Surface Charge.\u003ci\u003eR. Bone and D.A. Agard\u003c\/i\u003e, Mutational Remodeling of Enzyme Specificity.\u003ci\u003eL. Hedstrom, L. Grath, C.B. Stewart, W.J. Rutter, and M.A. ~Phillips\u003c\/i\u003e, Modulation of Enzyme Specificity by Site-Directed Mutagenesis.\u003ci\u003eM.E. Wales and J.R. Wild\u003c\/i\u003e, Analysis of Structure-Function Relationships by Formation of Chimeric Enzymes Produced by Gene Fusion.\u003ci\u003eL.C. Kuo\u003c\/i\u003e, Generation of Allosteric Enzymes from Nonallosteric Forms.\u003ci\u003eI.T. Weber\u003c\/i\u003e, Modeling of Structure of HIV-1 Protease with Substrate Based on the Crystal Structure of RSV Protease.\u003ci\u003eR.L.P. Lindberg and M. Negishi\u003c\/i\u003e, Modulation of Specificity and Activity in Mammalian Cytochrome P450.\u003cb\u003eCross-Index to Prior Volumes:\u003c\/b\u003e\u003ci\u003eJ.T. Langone\u003c\/i\u003e, Related Chapters in Previous Methods in Enzymology Volumes.Each chapter includes references.Author Index.Subject Index.\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Computer science [\u003ca title=\"See our other books on Computer science\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Computer%20science%20%5BUY%5D%22\"\u003eUY\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Enzymology [\u003ca title=\"See our other books on Enzymology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Enzymology%20%5BPSBZ%5D%22\"\u003ePSBZ\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649190482200,"sku":"9780121821036","price":39.36,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780121821036_bacedbec-af96-474f-87b3-63159668451e.jpg?v=1695006657"},{"product_id":"regulators-and-effectors-of-small-gtpases-ras-family-hardback-9780121828127","title":"Regulators and Effectors of Small GTPases: Ras Family (Hardback) 9780121828127","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eRegulators and Effectors of Small GTPases: Ras Family\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eW. E. Balch (Volume editor), Channing J. Der (Volume editor), Alan Hall (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780121828127\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 7 June 2006\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e824 pages, Approx. 150 illustrations (50 in full color)\u003cbr\u003e22.9 x 15.1 x 4.1 cm, 1.22 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\u003cp\u003ePraise for the Series \u003c\/p\u003e \u003cp\u003e\"Incomparably useful.\" --\u003cb\u003eANALYTICAL BIOCHEMISTRY\u003c\/b\u003e \u003c\/p\u003e \u003cp\u003e\"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page.\" --\u003cb\u003eBIO\/TECHNOLOGY \u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection.\" --\u003cb\u003eCHEMISTRY IN INDUSTRY\u003c\/b\u003e\u003c\/p\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThe Ras superfamily (\u0026gt;150 human members) encompasses Ras GTPases involved in cell proliferation, Rho GTPases involved in regulating the cytoskeleton, Rab GTPases involved in membrane targeting\/fusion and a group of GTPases including Sar1, Arf, Arl and dynamin involved in vesicle budding\/fission. These GTPases act as molecular switches and their activities are controlled by a large number of regulatory molecules that affect either GTP loading (guanine nucleotide exchange factors or GEFs) or GTP hydrolysis (GTPase activating proteins or GAPs). In their active state, they interact with a continually increasing, functionally complex array of downstream effectors. Since the last \u003cb\u003eMethods in Enzymology\u003c\/b\u003e volume on this topic in 2000, the study of Ras Family GTPases has witnessed a plethora of new directions and trends. With regards to the founding member of the Ras superfamily, the study of Ras in oncogenesis has seen the development and application of more advanced model cell culture and animal systems. The discovery of mutationally activated B-Raf in human cancers has injected renewed interest in this classical effector pathway of Ras.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eReal-time in vitro measurement of Intrinsic and Ras GAP-mediated GTP hydrolysis; \u003cbr\u003eSchwann cell preparation from single mouse embryos: Analyses of neurofibromin function in Schwann cells; Regulation of the nucleotide state of oncogenic Ras proteins by nucleoside diphosphate kinase; Measurements of TSC2 GAP activity toward Rheb; Characterization of AND-34 function and signalling; Studying the spatial and temporal regulation of Ras GTPase-activating proteins; Activation of Ras Proteins by Ras Guanine Nucleotide Releasing Protein Family Members; Ras and Rap1 Activation of PLC? lipase activity; Specificity and expression of RalGPS as RalGEFs; Biochemical and biological analyses of Rgr RalGEF oncogene; Analysis of Ras Activation in Living Cells with GFP-RBD; Genetic and pharmacologic analyses of the role of Icmt in Ras membrane association and function; Characterization of the activation of the Rap specific exchange factor epac by cyclic nucleotides; Biochemistry of the Rap-specific guanine nucleotide exchange factors PDZ-GEF1 and 2; Characterization of interactions between Ras family GTPases and their effectors; Genetic and pharmacologic dissection of Ras effector utilization in oncogenesis; Sequencing analysis of BRAF mutations in human cancers; KSR regulation of the Raf-MEK-ERK cascade; Ras-sensitive IMP modulation of the Raf\/MEK\/ERK cascade through KSR1; Raf Kinase Inhibitor Protein (RKIP) regulation of Raf and MAPK signalling; Harnessing RNAi for Analyses of Ras Signaling and Transformation; The Rac Activator Tiam1and Ras induced Oncogenesis; Phospholipase Ce CƒÕ guanine nucleotide exchange factor activity and activation of Rap1; Nore1 and RASSF1 regulation of cell proliferation and of the MST1\/2 kinases; RASSF family proteins and Ras transformation; Ras and the Rain\/RasBP1 effector; The RIN family of Ras effectors; RAP1 regulation of RIAM and cell adhesion; Regulation of cell-cell adhesion by Rap1; Effects of Ras signaling on gene expression analyzed by customized microrays; Protein-fragment complementation assays (PCA) in small GTPase research and drug discovery; Ras Up-regulation of Cycloxygenase-2; Regulation of the expression of tropomyosins and actin cytoskeleton by ras-transformation; Regulation of Par-4 by Oncogenic Ras; Using Drosophila and yeast genetics to investigate a role for the RhebGTPase in cell growth; Biochemistry and Biology of ARHI (DIRAS3), An Imprinted Tumor Suppressor Gene Whose Expression Is Lost In Ovarian and Breast Cancer; Gem protein signaling and regulation; Analysis of Rem\/RGK Signaling and Biological Activity; Analysis of Rit Signaling and Biological Activity; Characterization of RERG: An estrogen-regulated tumor suppressor gene; Inhibition of transcription factor NF-?B activation by ?B-Ras; Analysis of Rhes activation state and effector function ; Rheb activation of mTOR and S6K1 signaling; Use of Retrovirus Expression of Interfering RNA to Determine the Contribution of Activated K-Ras and Ras Effector Expression to Human Tumor Cell Growth; Using inhibitors of prenylation to block localization and transforming activity; Sorafenib (BAY 43-9006), a dual action inhibitor that targets RAF\/MEK\/ERK pathway in tumor cells and tyrosine kinases VEGFR\/PDGFR in tumor vasculature; Yeast screens for inhibitors of Ras-Raf interaction and characterization of MCP inhibitors of Ras-Raf interaction; A tagging-via-substrate technology for genome-wide detection and identification of farnesylated proteins; A genetically defined normal human somatic cell system to study Ras oncogenesis in vivo and in vitro; Analyses of Ras transformation of human thyroid epithelial cells; Use of Ras-transformed human ovarian surface epithelial cells as a model for studying ovarian cancer; Physiological analysis of oncogenesic Kras; Use of conditionally active Ras Fusion Proteins to study Epidermal Growth, Differentiation and Neoplasia; Pancreatic duct epithelial cell isolation and cultivation in two dimensional and three dimensional culture systems; Analyses of RAS regulation of eye development in Drosophila melanogaster; Ras superfamily and interacting proteins database\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46649193267480,"sku":"9780121828127","price":91.59,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780121828127_d9ce9344-5d7d-491b-85f9-dbf26aae882d.jpg?v=1694352018"},{"product_id":"ubiquitin-and-protein-degradation-part-b-hardback-9780121828042","title":"Ubiquitin and Protein Degradation, Part B (Hardback) 9780121828042","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eUbiquitin and Protein Degradation, Part B\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThe newest volume in the critically acclaimed laboratory standard \u003ci\u003eMethods in Enzymology\u003c\/i\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRaymond J. Deshaies (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780121828042, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 4 November 2005\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e952 pages\u003cbr\u003e22.9 x 15.1 x 4.6 cm, 1.43 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003ePraise for the Series:\u003cbr\u003e\"Incomparably useful.\" \u003cb\u003e--ANALYTICAL BIOCHEMISTRY\u003cbr\u003e\u003c\/b\u003e\u003cbr\u003e\"The Methods in Enzymology series represents the gold standard.\" \u003cb\u003e--NEUROSCIENCE\u003c\/b\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003ci\u003eUbiquitin and Protein Degradation, Part B\u003c\/i\u003e covers chemical biology, ubiquitin derivatives and ubiquitin-like proteins, deubiquitinating enzymes, proteomics as well as techniques to monitor protein degradation. The chapters are highly methodological and focus on application of techniques.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSECTION I.  UBIQUITIN AND UBIQUITIN DERIVATIVES\u003cbr\u003eSECTION II.  UBIQUITIN-BINDING DOMAINS\u003cbr\u003eSECTION III.  METHODS TO STUDY THE PROTEASOME\u003cbr\u003eSECTION IV.  IDENTIFICATION AND CHARACTERIZATION OF SUBSTRATES AND UBIQUITIN LIGASES \u003cbr\u003eSECTION V. GENOME- AND PROTEOME-WIDE APPROACHES TO IDENTIFY SUBSTRATES AND ENZYMES \u003cbr\u003eSECTION VI. REAL TIME\/NON-INVASIVE TECHNOLOGIES\u003cbr\u003eSECTION VII.  SMALL MOLECULE INHIBITORS\u003cbr\u003eSECTION VIII. GENERALLY APPLICABLE TECHNOLOGIES\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Enzymology [\u003ca title=\"See our other books on Enzymology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Enzymology%20%5BPSBZ%5D%22\"\u003ePSBZ\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649193496856,"sku":"9780121828042","price":105.69,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780121828042_28a95bc1-54aa-4638-a1b6-052cd5f8cb6b.jpg?v=1695006699"},{"product_id":"ion-channel-factsbook-voltage-gated-channels-paperback-9780121844530","title":"Ion Channel Factsbook; Voltage-Gated Channels (Paperback \/ softback) 9780121844530","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eIon Channel Factsbook\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eVoltage-Gated Channels\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eWilliam J. Brammar (Author)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780121844530, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePaperback \/ softback, published 16 October 1998\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e876 pages\u003cbr\u003e22.9 x 15.2 x 5.3 cm, 1.34 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThe Academic Press \u003cb\u003eFactsBooks\u003c\/b\u003e series has established itself as the best source of easily-accessible and accurate facts about protein groups. Described as 'a growing series of excellent manuals' by \u003ci\u003eMolecular Medicine Today\u003c\/i\u003e, and 'essential works of reference' by \u003ci\u003eTrends in Biochemical Sciences\u003c\/i\u003e, the \u003cb\u003eFactsBooks\u003c\/b\u003e have become the most popular comprehensive data resources available. As they are meticulously researched and use an easy-to-follow format, the \u003cb\u003eFactsBooks\u003c\/b\u003e will keep you up-to-date with the latest advances in structure, amino acid sequences, physicochemical properties, and biological activity.\u003cbr\u003eIn a set of four interrelated volumes, \u003cb\u003eThe Ion Channel FactsBook\u003c\/b\u003e provides a comprehensive framework of facts about channel molecules central to electrical signaling phenomena in living cells. The fourth volume is devoted to Voltage-gated Channel Families, including those molecular complexes activated or modulated by calcium, potassium, and chloride.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eCumulative table of contents from volumes I-IV.\u003cbr\u003eAcknowledgements.\u003cbr\u003eIntroduction and layout of entries.\u003cbr\u003eAbbreviations.\u003cbr\u003eVLG Key Facts.\u003cbr\u003eVLG Ca.\u003cbr\u003eVLG Cl.\u003cbr\u003eVLG K A-T (native).\u003cbr\u003eVLG K DR (native).\u003cbr\u003eVLG K Eag\/elk\/erg.\u003cbr\u003eVLG K Kv-beta.\u003cbr\u003eVLG K Kv1-Shak.\u003cbr\u003eVLG Kv2-Shab.\u003cbr\u003eVLG Kv3-Shaw.\u003cbr\u003eVLG Kv4-Shal.\u003cbr\u003eVLG K Kvx (unassigned),\u003cbr\u003eVLG K M-i (native), VL9 (K)minK Kvx.\u003cbr\u003eVLG K M-i. VLG(K)minK.\u003cbr\u003eCumulative Page Index.\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Reference works [\u003ca title=\"See our other books on Reference works\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Reference%20works%20%5BGBC%5D%22\"\u003eGBC\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649193759000,"sku":"9780121844530","price":59.96,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780121844530_1be739e6-01ba-4c5f-8e6d-49a7c52d1008.jpg?v=1695006672"},{"product_id":"heparin-binding-proteins-hardback-9780121860608","title":"Heparin-Binding Proteins (Hardback) 9780121860608","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eHeparin-Binding Proteins\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eH. Edward Conrad (Author)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780121860608, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 2 October 1997\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e527 pages\u003cbr\u003e22.9 x 15.1 x 3.1 cm, 0.93 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\"...a remarkable achievement... I found reading this book to be highly rewarding... highly valuable as an introduction to various aspects of heparin\/heparan sulfate chemistry and biology.\" --\u003cb\u003eUlf Lindahl, Unviersity of Uppsala, Sweden, in JOURNAL OF MEDICINAL CHEMISTRY (1999)\u003c\/b\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThis book describes the complex structures of heparins and heparan sulfates (heparinoids) and how they are generated by their biosynthetic pathways. The book also details the methodologies for studying these structures and their cellular metabolism. \u003cb\u003eHeparin-Binding Proteins\u003c\/b\u003e introduces the general nature of interactions between heparinoids and proteins, and presents the role for these structures in their interactions with the proteins of the hemostatic mechanisms, fibroblasts growth factors, superoxide dismutase, and lipoproteins.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePreface. Conventions, Abbreviations, And Terminology. Heparin Vs. Heparan Sulfate. Structures of Heparinoids. Experimental Approaches for Determining Heparinoid Structures. Structural Modification of Heparinoids. The Cellular Metabolism of Heparan Sulfate. Interactions Between Heparinoids and Proteins. Antithrombin: The Prototype for Heparin-Binding Proteins. Heparin-Binding Proteins in Hemostasis. Fibroblast Growth Factors. Extracellular Superoxide Dismutase. Heparin-Binding Proteins in Lipoprotein Metabolism. Epilog. Appendix: Other Heparin-Binding Proteins. Subject Index.\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Pharmacology [\u003ca title=\"See our other books on Pharmacology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Pharmacology%20%5BMMG%5D%22\"\u003eMMG\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649193988376,"sku":"9780121860608","price":104.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780121860608_82078e35-1c3c-4d59-b2b1-3954083df3f2.jpg?v=1695006710"},{"product_id":"regulators-and-effectors-of-small-gtpases-rho-family-hardback-9780121828110","title":"Regulators and Effectors of Small GTPases: Rho Family (Hardback) 9780121828110","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eRegulators and Effectors of Small GTPases: Rho Family\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eW. E. Balch (Volume editor), Channing J. Der (Volume editor), Alan Hall (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780121828110, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 21 February 2006\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e848 pages, Approx. 250 illustrations (50 in full color)\u003cbr\u003e22.9 x 15.1 x 4.2 cm, 1.29 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\u003cp\u003ePraise for the Series  \"Incomparably useful.\" --\u003cb\u003e\u003ci\u003eANALYTICAL BIOCHEMISTRY\u003c\/i\u003e\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page.\" --\u003cb\u003e\u003ci\u003eBIO\/TECHNOLOGY\u003c\/i\u003e\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection.\" --\u003cb\u003e\u003ci\u003eCHEMISTRY IN INDUSTRY\u003c\/i\u003e\u003c\/b\u003e\u003c\/p\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eThe Ras superfamily (\u0026gt;150 human members) encompasses Ras GTPases involved in cell proliferation, Rho GTPases involved in regulating the cytoskeleton, Rab GTPases involved in membrane targeting\/fusion and a group of GTPases including Sar1, Arf, Arl and dynamin involved in vesicle budding\/fission. These GTPases act as molecular switches and their activities are controlled by a large number of regulatory molecules that affect either GTP loading (guanine nucleotide exchange factors or GEFs) or GTP hydrolysis (GTPase activating proteins or GAPs). In their active state, they interact with a continually increasing, functionally complex array of downstream effectors.\u003c\/p\u003e  \u003cp\u003eSince the last \u003ci\u003eMethods in Enzymology\u003c\/i\u003e volume on this topic in 2000, Rho GTPases have continued to receive a huge amount of attention. The human genome sequence has revealed the full extent of the Rho GEF and Rho GAP families (over 80 members for each) and the challenge of identifying the molecular interactions and cellular pathways influenced by each of these regulators is a daunting prospect. This new volume, \u003ci\u003eRegulators and Effectors of Small GTPases: Rho Family\u003c\/i\u003e, describes some of the methods currently being used to examine Rho family GTPase regulation at the biochemical and cellular level.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePurification and Biochemical Properties of Rac1,2,3 and the Splice Variant Rac1b\u003cbr\u003e  Biochemical Analyses of the Wrch Atypical Rho Family GTPases\u003cbr\u003e  Purification of P-Rex1 from neutrophils and nucleotide exchange assay\u003cbr\u003e  In vitro guanine nucleotide exchange activity of DHR-2\/DOCKER\/ CZH2 domains\u003cbr\u003e Biochemical characterization of the Cool (Coned-out-of-Library)\/Pix (Pak-interactive exchange factor) proteins\u003cbr\u003e GEF and glucosylation assays on liposome bound Rac\u003cbr\u003e Phosphorylation of RhoGDI by p21-activated kinase 1\u003cbr\u003e Purification of ARAP3 and characterization of GAP activities\u003cbr\u003e Regulation of RhoGAP specificity by phospholipids and prenylation\u003cbr\u003e Purification and activity of the Rho ADP-ribosylating binary C2\/C3 toxin\u003cbr\u003e  Purification of Tat-C3 exoenzymes\u003cbr\u003e Imaging and photobleach correction of MeroCBD,  sensor of endogenous Cdc42 activation \u003cbr\u003e Cdc42 and PI(4,5)P2-induced actin assembly in Xenopus egg extracts\u003cbr\u003e In Vitro Reconstitution of Cdc42-Mediated Actin Assembly Using Purified Components\u003cbr\u003e Biochemical Analysis of Mammalian Formin Effects on Actin Dynamics\u003cbr\u003e Formin proteins: purification and measurement of effects on actin assembly\u003cbr\u003e Purification and Kinase Assay of PKN\u003cbr\u003e Purification and Enzyme Activity of ACK1\u003cbr\u003e Direct activation of purified phospholipase C epsilon by RhoA studied in  reconstituted phospholipid vesicles\u003cbr\u003e Regulation of PLCâ isoforms by Rac\u003cbr\u003e Biochemical properties and inhibitors of (N-)WASP\u003cbr\u003e The Use of GFP to localize Rho GTPases in Living Cells\u003cbr\u003e Analysis of the Spatio-Temporal Activation of Rho GTPases using Raichu Probes\u003cbr\u003e Measurement of Activity of Rho GTPases during Mitosis\u003cbr\u003e RNAi inhibition of Rho GTPases\u003cbr\u003e RNA interference techniques to study epithelial cell adhesion and polarity\u003cbr\u003e Nucleofection of primary neurons\u003cbr\u003e Dock180-ELMO Cooperation in Rac Activation\u003cbr\u003e Rho GTPase activation by cell-cell adhesion\u003cbr\u003e Activation of Rap1, Cdc42, and Rac by nectin adhesion system\u003cbr\u003e Analysis of activated GAPs and GEFs in cell lysates\u003cbr\u003e Degradation of RhoA by Smurf1 ubiquitin ligase\u003cbr\u003e Ubiquitin-mediated proteasomal degradation of Rho proteins by the CNF1 toxin\u003cbr\u003e Regulation of superoxide-producing NADPH in non-phagocytic cells\u003cbr\u003e Activation of MEKK1 by Rho GTPases\u003cbr\u003e Activation of Apoptotic JNK Pathway through the Rac1-Binding Scaffold Protein POSH\u003cbr\u003e Quantification of isozyme-specific activation of phospholipase C-â2 by Rac GTPases and phospholipase C-å by Rho GTPases in an intact cell assay system\u003cbr\u003e Activation of Rho and Rac by Wnt\/Frizzled  signalling\u003cbr\u003e Fluorescent assay of cell permeable C3 transferase activity\u003cbr\u003e Use of TIRF microscopy to visualize actin and microtubules in migrating cells\u003cbr\u003e Inhibition of ROCK by RhoE\u003cbr\u003e Conditional regulation of a ROCK-estrogen receptor fusion protein\u003cbr\u003e Rational design and applications of a Rac GTPase-specific small molecule inhibitor\u003cbr\u003e In vitro assay of primary astrocyte migration as a tool to study Rho GTPase function in cell polarization\u003cbr\u003e Real time centrosome reorientation during fibroblast migration\u003cbr\u003e Lentiviral delivery of RNAi in Hippocampal Neurons\u003cbr\u003e Methods for studying neutrophil Chemtoaxis\u003cbr\u003e Measurement of Epidermal Growth Factor Receptor turnover and effects of Cdc42\u003cbr\u003e Tumor cell migration in three dimensions\u003cbr\u003e Reciprocal regulation of cyclin D1 expression by Rac and Rho\u003cbr\u003e Regulation of ERK signal duration and cyclin D1 expression by Rhodependent stress fiber formation\u003cbr\u003e An in vitro model to study the role of endothelial Rho GTPases during leukocyte transendothelial migration\u003cbr\u003e Analysis of a Mitotic role of Cdc42\u003cbr\u003e Plexin-induced collapse assay in COS cells\u003cbr\u003e Morphological and Biochemical Analysis of Rac1 in Three-Dimensional Epithelial Cell Cultures\u003cbr\u003e Using Three Dimensional Acinar Structures for Molecular and Cell Biological Assays\u003cbr\u003e TC10 and insulin-stimulated glucose transport\u003cbr\u003e GTPases and the control of neuronal polarity\u003cbr\u003e In vitro assembly of filopodia-like bundles\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649195266328,"sku":"9780121828110","price":91.59,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780121828110_3deaad60-3dcd-4fab-be57-5619df890cf0.jpg?v=1695006667"},{"product_id":"protein-physics-a-course-of-lectures-hardback-9780122567810","title":"Protein Physics; A Course of Lectures (Hardback) 9780122567810","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProtein Physics\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eA Course of Lectures\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eAlexei V. Finkelstein (Author)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780122567810, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 7 May 2002\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e354 pages\u003cbr\u003e22.9 x 15.1 x 2.5 cm, 0.68 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\"It is not always easy to translate a good lecture course into an equally engaging textbook, but Finkelstein and Ptitsyn have succeeded in this difficult task. The twenty-five chapters are not only an accurate and detailed introduction to the physics of proteins, but also remarkably lively. ...the book is a pleasure to read and is well suited both as a textbook used in a course on protein science and as a tool for self-study.\" \u003cb\u003e--Ulrich H. E. Hansmann for the BULLETIN OF MATHEMATICAL BIOLOGY, Sept. 2003\u003c\/b\u003e\u003cbr\u003e\u003cbr\u003e\"The lectures are unique... anticipating questions from the students, and answering them, with an interspersion of simple examples...a good introduction to protein physics for students, ...will help chemists, physicists, and biologists acquire a widespread knowledge of current issues in protein structure, properties, and reactions.\" \u003cb\u003e--Harold A. Scheraga, Todd Professor of Chemistry, Cornell University, USA\u003c\/b\u003e\u003cbr\u003e\u003cbr\u003e\"Protein Physics provides all the essential information. ...concise, reliable and very well written\" \u003cb\u003e--Israel M. Gelfand, Distinguished Professor Rutgers University, USA\u003c\/b\u003e\u003cbr\u003e\u003cbr\u003e\"Rigorous and thorough analysis of physical basis of protein structure...unique in its profound professionalism ... free, colloquial style.\" \u003cb\u003e--Alexander S. Spirin, Professor of Biochemistry, Moscow University, Russia\u003c\/b\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003ci\u003eProtein Physics\u003c\/i\u003e is a lively presentation of the most general problems of protein structure, folding and function from the physics and chemistry perspective, based on lectures given by the authors. It deals with fibrous, membrane and, most of all, with the best studied water-soluble globular proteins, in both their native and denatured states. The major aspects of protein physics are covered systematically, physico-chemical properties of polypeptide chains; their secondary structures; tertiary structures of proteins and their classification; conformational transitions in protein molecules and their folding; intermediates of protein folding; folding nuclei; physical backgrounds of coding the protein structures by their amino acid sequences and protein functions in relation to the protein structure. The book will be of interest to undergraduate and graduate level students and researchers of biophysics, biochemistry, biology and material science.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eElementary Interactions in Proteins and Around\u003cbr\u003eSecondary Structures of Polypeptide Chains\u003cbr\u003eProtein Structures\u003cbr\u003eCooperative Transitions in Protein Molecules\u003cbr\u003eProtein Structure Prediction and Design\u003cbr\u003eProtein Functions\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Natural history [\u003ca title=\"See our other books on Natural history\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Natural%20history%20%5BWN%5D%22\"\u003eWN\u003c\/a\u003e], Animal husbandry [\u003ca title=\"See our other books on Animal husbandry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Animal%20husbandry%20%5BTVH%5D%22\"\u003eTVH\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biology, life sciences [\u003ca title=\"See our other books on Biology, life sciences\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biology,%20life%20sciences%20%5BPS%5D%22\"\u003ePS\u003c\/a\u003e], Chemistry [\u003ca title=\"See our other books on Chemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Chemistry%20%5BPN%5D%22\"\u003ePN\u003c\/a\u003e], Chemical physics [\u003ca title=\"See our other books on Chemical physics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Chemical%20physics%20%5BPHVQ%5D%22\"\u003ePHVQ\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Applied physics [\u003ca title=\"See our other books on Applied physics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Applied%20physics%20%5BPHV%5D%22\"\u003ePHV\u003c\/a\u003e], Atomic \u0026amp; molecular physics [\u003ca title=\"See our other books on Atomic \u0026amp; molecular physics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Atomic%20\u0026amp;%20molecular%20physics%20%5BPHM%5D%22\"\u003ePHM\u003c\/a\u003e], Physics [\u003ca title=\"See our other books on Physics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Physics%20%5BPH%5D%22\"\u003ePH\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649197658392,"sku":"9780122567810","price":60.76,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780122567810_d35bc442-9add-475e-8acb-e7c940a60cb8.jpg?v=1695006710"},{"product_id":"the-transporter-factsbook-paperback-9780123039651","title":"The Transporter Factsbook (Paperback \/ softback) 9780123039651","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eThe Transporter Factsbook\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eJeffrey Griffith (Author), Clare Sansom (Author)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123039651, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePaperback \/ softback, published 22 December 1997\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e508 pages\u003cbr\u003e22.9 x 15.1 x 3.2 cm, 0.85 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eHow do you keep track of basic information on the proteins you work with? Where do you find details of their physicochemical properties, amino acid sequences, and structure? Are you tired of scanning review articles, primary papers, and databases to locate that elusive fact? The Academic Press FactsBook Series has established itself as the best source of easily-accessible and accurate facts about protein groups. Described as \"a growing series of excellent manuals\" by \u003ci\u003eMolecular Medicine Today\u003c\/i\u003e and \"essential works of reference\" by \u003ci\u003eTrends in Biochemical Sciences\u003c\/i\u003e, the FactsBooks have become the most popular comprehensive data resources available. Using an easy-to-follow format, the FactsBooks will keep you up-to-date with the latest advances in structure, amino acid sequences, physicochemical properties, and biological activity. Meticulously researched and compiled by experts in the field, keeping abreast of developments has never been so easy!\u003cb\u003eThe Transporter FactsBook\u003c\/b\u003e contains entries covering almost 800 transporters. Organized into 55 families of structurally related transporters, this volume includes ATPases, ABC transporters, H+-dependent antiporters and symporters, Na+-dependent antiporters and symporters, and other transporters such as mitochondrial transporters.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cb\u003eIntroductory Chapters:\u003c\/b\u003eFunction and Structure of Membrane Transport Proteins.Amino Acid Sequence Comparisons.Organization of the Data.\u003cb\u003eThe Membrane Transport Proteins:\u003c\/b\u003e\u003cb\u003eP-Type ATPases:\u003c\/b\u003eCalcium-transporting ATPase Family.Plasma Membrane Cation-transporting ATPase Family.Heavy Metal-transporting ATPase Family.\u003cb\u003eVacuolar ATPases:\u003c\/b\u003eVacuolar ATPase family.\u003cb\u003eABC Multidrug Resistance Proteins:\u003c\/b\u003eWhite transporter family.ABC 1 \u0026amp; 2 transporter family.Yeast multidrug resistance family.Cystic fibrosis transmembrane conductance regulator family.P-Glycoprotein transporter family.Peroxisomal membrane transporter family.\u003cb\u003eABC-2 Transporters:\u003c\/b\u003eABC-2 nodulation protein family.ABC-2 polysaccharide exporter family.ABC-2 associated (cytoplasmic) protein family.\u003cb\u003eABC Binding Protein-Dependent Transporters: Transmembrane Elements:\u003c\/b\u003eABC-associated binding protein-dependent maltose transporter family.ABC-associated binding protein-dependent peptide Transporter Family.ABC-associated binding protein-dependent iron transporter family.\u003cb\u003eABC Binding Protein-Dependent Transporters: Cytoplasmic Elements:\u003c\/b\u003eBinding protein-dependent monosaccharide transporter family.Binding protein-dependent peptide transporter family.\u003cb\u003eOther ABC-Associated (Cytoplasmic) Proteins:\u003c\/b\u003eHeme exporter family.Macrolide-streptogrammin-tylosin resistance family.\u003cb\u003eH+-Dependent Symporters:\u003c\/b\u003eH+\/sugar-symporter-uniporter family.H+\/sugar-symporter-uniporter family.H+\/Rhamnose symporter family.H+\/amino acid symporter family.H+\/lactose-sucrose-nucleoside symporter family.H+\/galactoside-pentose-hexuronide symporter family.H+\/oligopeptide symporter family.H+\/fucose symporter family.H+\/carboxylate symporter family.H+\/nucleotide symporter family.Sugar phosphate transporter family.\u003cb\u003eH+-Dependent Antiporters:\u003c\/b\u003eH+-vesicular amine antiporter family.14-helix H+\/multidrug antiporter family.4-helix H+\/multidrug antiporter family.12-helix H+\/multidrug antiporter family.Acriflavin-cation resistance family.Yeast multidrug resistance family.\u003cb\u003eNa+-Dependent symporters:\u003c\/b\u003eNa+\/Ca\u003csup\u003e+2\u003c\/sup\u003e exchanger family.Na+\/proline symporter family.Na+\/glucose symporter family.Na+\/dicarboxylate symporter family.Na+\/P04 symporter family.Na+\/branched amino acid symporter family.Na+\/citrate symporter family.Na+\/alanine-glycine symporters.Na+\/neurotransmitter symporters.\u003cb\u003eNa+-Dependent antiporters:\u003c\/b\u003eNa+\/H+ antiporter family.\u003cb\u003ePEP-Dependent phophotransferase family:\u003c\/b\u003ePEP-Phosphoenolpyruvate-dependent sugar phophotransferase family.\u003cb\u003eOther Transporters:\u003c\/b\u003eAnion exchanger family.Mitochondrial adenine nucleotide translocator family.Mitochondrial phosphate carrier family.Nitrate transporter I family.Nitrate transporter II family.Spore germination transporter family.Vacuolar membrane pyrophosphatase family.Gluconate transporter family.Index.\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649199100184,"sku":"9780123039651","price":41.77,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123039651_3139dcdf-4234-436b-8927-006a8288b334.jpg?v=1695006722"},{"product_id":"neuropeptide-y-and-drug-development-hardback-9780123049902","title":"Neuropeptide Y and Drug Development (Hardback) 9780123049902","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eNeuropeptide Y and Drug Development\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eLars Grundemar (Edited by), Stephen R. Bloom (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123049902, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 15 November 1996\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e209 pages\u003cbr\u003e22.9 x 15.1 x 2 cm, 0.48 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\u003ci\u003eNeuropeptide Y (NPY)\u003c\/i\u003e is a ubiquitous and important messenger in the nervous system, with a wide range of physiological roles. It is involved in the body energy balance and is one of the most potent stimuli of food intake known. NPY also acts to regulate central and peripheral autonomic functions.\u003c\/p\u003e  \u003cp\u003eThis book, written by academic and industrial experts in the field, links the most recent basic experimental knowledge about NPY and its receptors with areas of clinical importance.\u003c\/p\u003e  \u003cp\u003eThis book will be of interest to those working in all areas of research affected by NPY, such as food intake and energy homeostasis, cardiovascular regulation and G-protein-coupled receptors, as well as those interested in the development of drugs as NPY targets.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eMultiple Receptors and Multiple Actions Central Effects of Neuropeptide Y and Its Role in Obesity and Diabetes Neuropeptide Y in Sympathetic Nerves-Evidence for Y1 Receptor-Mediated Vascular Control Neuropeptide Y Receptor Types in Mammalian Brain Species Differences and Status in the Human Central Nervous System Extraordinary Structural Diversity of Neuropeptide Y Family Receptors The Importance of Various Parts of the Neuropeptide Y Molecule for Receptor Recognition Peptide Antagonists of Neuropeptide Y: Design, Structure, And Pharmacological Characterization SR 120819A or the First Generation of Orally-Active Neuropeptide Y1 Receptor Antagonists BIBP3226, A Potent and Selective Y1 Receptor Antagonist First Structure-Activity Studies and Localization of the Human Y1 Receptor Binding Site Discovery of Neuropeptide Y Receptor Antagonists \u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Pharmaceutical technology [\u003ca title=\"See our other books on Pharmaceutical technology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Pharmaceutical%20technology%20%5BTDCW%5D%22\"\u003eTDCW\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Neurosciences [\u003ca title=\"See our other books on Neurosciences\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Neurosciences%20%5BPSAN%5D%22\"\u003ePSAN\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Pharmacology [\u003ca title=\"See our other books on Pharmacology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Pharmacology%20%5BMMG%5D%22\"\u003eMMG\u003c\/a\u003e], Endocrinology [\u003ca title=\"See our other books on Endocrinology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Endocrinology%20%5BMJG%5D%22\"\u003eMJG\u003c\/a\u003e], Physiology [\u003ca title=\"See our other books on Physiology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Physiology%20%5BMFG%5D%22\"\u003eMFG\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649200869656,"sku":"9780123049902","price":114.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123049902_464bb051-3d9c-407b-bd91-ca71ed595500.jpg?v=1695006756"},{"product_id":"membrane-protein-purification-and-crystallization-a-practical-guide-paperback-9780123617767","title":"Membrane Protein Purification and Crystallization; A Practical Guide (Paperback \/ softback) 9780123617767","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eMembrane Protein Purification and Crystallization\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eA Practical Guide\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eCarola Hunte (Edited by), Gebhard von Jagow (Edited by), Hermann Schagger (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123617767\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePaperback \/ softback, published 5 January 2003\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e316 pages\u003cbr\u003e23.4 x 19 x 2.4 cm, 0.59 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThis second edition of \u003ci\u003eMembrane Protein Purification and Crystallization, A Practical Guide\u003c\/i\u003e is written for bench scientists working in the fields of biochemistry, biology, and proteomic research. This guide presents isolation and crystallization techniques in a concise form, emphasizing the critical aspects unique to membrane proteins. It explains the principles of the methods and provides protocols of general use, permitting researchers and students new to this area to adapt these techniques to their particular needs. This edition is not only an update but is comprised mainly of new contributions. It is the first monograph compiling the essential approaches for membrane protein crystallization, and emphasizes recent progress in production and purification of recombinant membrane proteins.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\u003cb\u003eI. Strategies and Techniques\u003c\/b\u003e Purification Strategies for Membrane Proteins Chromatographic Techniques and Basic Operations in Membrane Protein Purification Production and purification of recombinant membrane proteins SDS Electrophoresis Techniques Blue-Native Electrophoresis Preparative Isoelectric Focussing Membrane protein crystallization\u003c\/p\u003e \u003cp\u003e\u003cb\u003eII. Discussion of Selected Isolation Protocols\u003c\/b\u003e Lipid Dependent Inactivation and Reactivation of Bovine complex III Purification of affinity-epitope tagged G-protein coupled receptors Purification of NhaA, the Na+\/H+ Antiporter of Escherichia coli for 3D or 2D Crystallization Purification of the yeast cytochrome bc1 complex\u003c\/p\u003e \u003cp\u003e\u003cb\u003eIII. Crystallization of Membrane Proteins\u003c\/b\u003e Antibody fragment-mediated crystallization of membrane proteins Crystallization of Wolinella succinogenes quinol:fumarate reductase Ba3-type cytochrome-c oxidase from Thermus thermophilus purification, crystallization, and crystal transformation Two-dimensional crystallization of membrane proteins: a practical guide In cubo crystallization of membrane proteins\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46649204277528,"sku":"9780123617767","price":80.85,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123617767_06f25d94-0521-4780-8dbd-860a26214f6a.jpg?v=1694352034"},{"product_id":"fluorescent-proteins-hardback-9780123725585","title":"Fluorescent Proteins (Hardback) 9780123725585","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eFluorescent Proteins\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003ePresents current applications of autofluorescent proteins in cell and molecular biology.\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eKevin F. 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Molecular applications are addressed in chapters that detail work with single molecules, approaches to generating protein fusions and biosensors as well as analysis of protein-protein interactions in vivo by FRET, fluorescence polarization and fluorescence cross correlation techniques. A number of approaches to in vivo dynamics are presented, including FRAP, photoactivation, and 4-dimensional microscopy. Behavior of spindle components, membrane proteins, mRNA trafficking as well as analysis of cell types in tissues and in development are detailed and provide models for a wide variety of experimental approaches. In addition, several chapters deal directly with the computational issues involved in processing multidimensional image data and using fluorescent imaging to probe cellular behavior with quantitative modeling. 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Using Fluorescent Proteins to Study mRNA Trafficking in Living Cells 13. Visualising mRNA Localisation and Local Protein Translation in Neurons 14. Quantitative FRAP in Analysis of Molecular Binding Dynamics In Vivo  15. Quantitative and Qualitative Analysis of Plant Membrane Traffic Using Fluorescent Proteins 16. Engineering FRET Constructs Using CFP and YFP 17. Fluorescence Anisotropy Imaging Microscopy (FAIM) for homo-FRET in Living Cells 18. FRET by Fluorescence Polarization Microscopy 19. Bimolecular Fluorescence Complementation Visualization of Molecular Interactions in Living Cells 20. Protein-protein interactions determined by fluorescence correlation spectroscopy 21. Recent Advances on In Vivo Imaging with Fluorescent Proteins 22. Computational Processing and Analysis of Dynamic Image Data 23. Automated Classification of Mitotic Phenotypes of Human Cells Using Fluorescent Proteins 24. 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At the same time it provides generalists with a complete overview and offers insights into topics for more in-depth reading.\u003c\/p\u003e  \u003cp\u003eCovering areas that are receiving attention from people of many fields -- genomics, functional foods -- and including the latest research and developments in milk-protein phenomenon and interactions, this book will be an ideal resource for professionals and students alike.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eCh 1-Milk-An OverviewCh 2-The Comparative Genomics of Tammar Wallaby and Cape Fur Seal Lactation: Models to Examine Function of Milk ProteinsCh 3-Significance, Origin and Function of Bovine Milk Proteins: The Biological Implications of Manipulation or ModificationCh 4-Post Translational Modifications of CaseinsCh 5-Casein Micelle Structure and StabilityCh 6-Structure and Stability of Whey ProteinsCh 7-High Pressure-induced Interactions Involving Whey ProteinsCh 8-The Whey Proteins in Milk: Thermal Denaturation, Physical Interactions and Functional Properties of MilkCh 9-Effect of Drying on Milk ProteinsCh 10-Changes in Milk Proteins During Storage of Dry PowdersCh 11-Interactions and Functionality of Milk Proteins in Food EmulsionsCh 12-Milk Protein-Polysaccharide InteractionsCh 13-Interactions between Milk Proteins and MicronutrientsCh 14-Model Food Systems and Protein FunctionalityCh 15-Sensory Aspects of Dairy ProteinsCh 16-Milk Protein GelsCh 17-Nutritional and Functional Aspects of Dairy ProteinsCh 18-Milk Proteins: The Future\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Dairy farming [\u003ca title=\"See our other books on Dairy farming\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Dairy%20farming%20%5BTVHF%5D%22\"\u003eTVHF\u003c\/a\u003e], Food \u0026amp; beverage technology [\u003ca title=\"See our other books on Food \u0026amp; beverage technology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Food%20\u0026amp;%20beverage%20technology%20%5BTDCT%5D%22\"\u003eTDCT\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46649283019032,"sku":"9780123740397","price":82.19,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123740397.jpg?v=1694099496"},{"product_id":"non-natural-amino-acids-hardback-9780123743107","title":"Non-Natural Amino Acids (Hardback) 9780123743107","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eNon-Natural Amino Acids\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThis volume aims to provide fundamental insights into how proteins work within the context of complex biological systems of biomedical interest\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eTom W. Muir (Volume editor), John N. Abelson (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123743107, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 22 September 2009\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e350 pages\u003cbr\u003e22.9 x 15.1 x 2.5 cm, 0.63 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eBy combining the tools of organic chemistry with those of physical biochemistry and cell biology, \u003ci\u003eNon-Natural Amino\u003c\/i\u003e \u003ci\u003eAcids\u003c\/i\u003e aims to provide fundamental insights into how proteins work within the context of complex biological systems of biomedical interest.\u003c\/p\u003e  \u003cp\u003eThe critically acclaimed laboratory standard for 40 years, \u003ci\u003eMethods in Enzymology\u003c\/i\u003e is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. With more than 400 volumes published, each \u003ci\u003eMethods in Enzymology\u003c\/i\u003e volume presents material that is relevant in today's labs -- truly an essential publication for researchers in all fields of life sciences. \u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e(Tentative)\u003cbr\u003e1. Protein Engineering with the Traceless Staudinger Ligation (Ronald T. Raines and Annie Tam)\u003cbr\u003e\u003cbr\u003e2. Mechanistic studies of RNR using unnatural amino acids and semisynthesis (Joann Stubbe)\u003cbr\u003e\u003cbr\u003e3. Using Expressed Protein Ligation to Probe the Substrate Specificity of Lantibiotic Synthetases (Wilfred van der Donk and Xingang Zhang)\u003cbr\u003e\u003cbr\u003e4. Protein Phosphorylation by Semisynthesis: From Paper to Practice (Phlip A. Cole,Lawrence M. Szewczuk, and Mary Katherine Tarrant)\u003cbr\u003e\u003cbr\u003e5. Mechanistic studies of semisynthetic ion channels (Francis Valiyaveetil)\u003cbr\u003e\u003cbr\u003e6. Semi-synthesis of proteins using split inteins (Henning D. Mootz, Christina Ludwig, Joachim Zettler, Daniel Garbe)\u003cbr\u003e\u003cbr\u003e7. Segmental Isotopic Labeling of Proteins for Nuclear Magnetic Resonance (David Cowburn, Dongsheng Liu, Rong Xu)\u003cbr\u003e\u003cbr\u003e8. Use of intein-mediated protein ligation strategies for the fabrication of functional protein arrays (Shao Q Yao, Souvik Chattopadhaya, Farhana B. Abu Bakar)\u003cbr\u003e\u003cbr\u003e9. Expressed Protein Ligation for Metalloprotein Design and Engineering (Yi Lu, Wilfred van der Donk, Kenneth Clark)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649286263064,"sku":"9780123743107","price":98.29,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123743107.jpg?v=1694099517"},{"product_id":"globins-and-other-nitric-oxide-reactive-proteins-part-b-hardback-9780123742780","title":"Globins and Other Nitric Oxide-Reactive Proteins, Part B (Hardback) 9780123742780","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eGlobins and Other Nitric Oxide-Reactive Proteins, Part B\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eA collection of methods for researchers working in the lab and classroom alike.\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRobert K. Poole (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123742780, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 5 June 2008\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e712 pages, Approx. 160 illustrations (50 in full color)\u003cbr\u003e22.9 x 15.1 x 3.7 cm, 1.09 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThe critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with over 400 volumes (all of them still in print), the series contains much material still relevant today—truly an essential publication for researchers in all fields of life sciences. \u003cb\u003eMethods in Enzymology\u003c\/b\u003e is now available online at ScienceDirect — full-text online of volumes 1 onwards. For more information about the Elsevier Book Series on ScienceDirect Program, please visit: http:\/\/www.info.sciencedirect.com\/bookseries\/ This volume is the second of two planned volumes on the topic of globin and other nitric oxide-reactive proteins.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSection I.  Nitric Oxide-Metabolising and Detoxifying Enzymes\u003cbr\u003e\u003cbr\u003eChapter 1\u003cbr\u003eStructural Studies on Flavodiiron Proteins \u003cbr\u003eJoão B. Vicente, Maria Arménia Carrondo, Miguel Teixeira and Carlos Frazão\u003cbr\u003e\u003cbr\u003eChapter 2\u003cbr\u003eBiochemical, Spectroscopic and Thermodynamic Properties of Flavodiiron Proteins\u003cbr\u003eJoão B. Vicente, Marta C. Justino, Vera L. Gonçalves, Lígia M. Saraiva and Miguel Teixeira\u003cbr\u003e\u003cbr\u003eChapter 3\u003cbr\u003eKinetic Characterization of the Escherichia coli Nitric Oxide Reductase Flavorubredoxin \u003cbr\u003eJoão B. Vicente, Francesca M. Scandurra, Elena Forte, Maurizio Brunori, Paolo Sarti, Miguel Teixeira and Alessandro Giuffrè\u003cbr\u003e\u003cbr\u003eChapter 4\u003cbr\u003eEscherichia coli cytochrome c-nitrite reductase NrfA\u003cbr\u003eThomas A. Clarke, Paul C. Mills, Susie R. Poock, Julea N. Butt1, Myles R. Cheesman,  Jeffrey A. Cole, Jay C. D. Hinton, Andrew M. Hemmings, Gemma Kemp, Christopher Söderberg, Stephen Spiro, Jessica Van Wonderen, David J. Richardson\u003cbr\u003e\u003cbr\u003eChapter 5\u003cbr\u003eThe respiratory NO reductase (NorBC) from Paracoccus denitrificans\u003cbr\u003eSarah J. Field, Faye H. Thorndycroft, Andrey D. Matorin, \u003cbr\u003eDavid J. Richardson and Nicholas J. Watmough\u003cbr\u003e\u003cbr\u003eChapter 6\u003cbr\u003eRedox-controlled dinitrosyl formation at the diiron-oxo center of NorA\u003cbr\u003eRainer Cramm, Katja Strube\u003cbr\u003e\u003cbr\u003eChapter 7\u003cbr\u003ePurification and functional analysis of fungal nitric oxide reductase cytochrome P450nor\u003cbr\u003eLi Zhangand Hirofumi Shoun \u003cbr\u003e\u003cbr\u003eChapter 8 \u003cbr\u003eA Quantitative approach to nitric oxide inhibition of terminal oxidases of the respiratory chain \u003cbr\u003eMaria G. Mason, Rebecca S. Holladay, Peter Nicholls, Mark Shepherd and Chris E. Cooper\u003cbr\u003e\u003cbr\u003eSection II. Sensor Proteins\u003cbr\u003eChapter 9\u003cbr\u003eCloning, Expression, and Purification of the N-terminal Heme Binding Domain of the Globin-Coupled Sensors\u003cbr\u003eJennifer A. Saito, Tracey Allen K. Freitas, and Maqsudul Alam\u003cbr\u003e\u003cbr\u003eChapter 10\u003cbr\u003eOxygen-Sensing Histidine-Protein Kinases:  Assays of Ligand-Binding and Turnover of Response-Regulator Substrates\u003cbr\u003eMarie-Alda Gilles-Gonzalez, Gonzalo Gonzalez, Eduardo H. S. Sousa, and Jason Tuckerman\u003cbr\u003e\u003cbr\u003eChapter 11\u003cbr\u003eReactions of nitric oxide and oxygen with FNR (regulator of Fumarate and Nitrate Reduction), a global transcriptional regulator, during anaerobic growth of Escherichia coli\u003cbr\u003eJason C. Crack, Nick E. Le Brun, Andrew J. Thomson, Jeffrey Green and Adrian J. Jervis\u003cbr\u003e\u003cbr\u003eChapter 12\u003cbr\u003eGenome wide identification of binding sites for the nitric oxide sensitive transcriptional regulator NsrR.  \u003cbr\u003eSam Efromovich, David Grainger, Diane Bodenmiller, and Stephen Spiro.\u003cbr\u003e\u003cbr\u003eChapter 13\u003cbr\u003eMethods in Enzymology: Globins and other NO-reactive proteins.  Characterization of the NO-reactive transcriptional activator NorR.\u003cbr\u003eBenoît D’Autréaux, Nick Tucker, Stephen Spiro and Ray Dixon\u003cbr\u003e\u003cbr\u003eSection III.  Advanced Spectroscopic Methods\u003cbr\u003e\u003cbr\u003eChapter 14\u003cbr\u003eHemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni: A Comparative Study with Resonance Raman Spectroscopy  \u003cbr\u003eChangyuan Lu, Tsuyoshi Egawa, Masahiro Mukai, Robert K. Pooleand Syun-Ru Yeh\u003cbr\u003e\u003cbr\u003eChapter 15\u003cbr\u003eThe power of using continuous-wave and pulsed electron paramagnetic resonance methods for the structure analysis of the ferric forms and NO-ligated ferrous forms of globins.\u003cbr\u003eSabine Van Doorslaer and Filip Desmet\u003cbr\u003e\u003cbr\u003eChapter 16\u003cbr\u003eOxygen binding to haem proteins in solution, encapsulated in silica gels and in the crystalline state\u003cbr\u003eLuca Ronda, Stefano Bruno, Serena Faggiano, Stefano Bettati and Andrea Mozzarelli\u003cbr\u003e\u003cbr\u003eChapter 17\u003cbr\u003eCharacterization of ligand migration mechanisms inside haemoglobins from the analysis of geminate rebinding kinetics\u003cbr\u003eStefania Abbruzzetti, Stefano Bruno, Serena Faggiano, Luca Ronda, Elena Grandi, Andrea Mozzarelli, Cristiano Viappiani\u003cbr\u003e\u003cbr\u003eChapter 18\u003cbr\u003eLigand Dynamics in Heme Proteins Observed by \u003cbr\u003eFourier Transform Infrared Spectroscopy at Cryogenic Temperatures\u003cbr\u003eKarin Nienhaus, G. Ulrich Nienhaus\u003cbr\u003e\u003cbr\u003eChapter 19\u003cbr\u003eTime-resolved x-ray crystallography of heme proteins\u003cbr\u003eVukica Šrajer and William E. Royer, Jr\u003cbr\u003e\u003cbr\u003eChapter 20\u003cbr\u003eStructural Dynamics of Myoglobin\u003cbr\u003eMaurizio Brunori, Dominque Bourgeois and Beatrice Vallone\u003cbr\u003e\u003cbr\u003eChapter 21\u003cbr\u003eUse of the Conjugate Peak Refinement Algorithm for Identification of Ligand Binding Pathways in Globins\u003cbr\u003eStephen D. Golden and Kenneth W. Olsen\u003cbr\u003e\u003cbr\u003eChapter 22\u003cbr\u003eFinding gas migration pathways in proteins using implicit ligand sampling\u003cbr\u003eJordi Cohen, Kenneth W Olsen, and Klaus Schulten\u003cbr\u003e\u003cbr\u003eChapter 23\u003cbr\u003eIdentification of Ligand Binding Pathways in Truncated Hemoglobins Using Locally Enhanced Sampling Molecular Dynamics\u003cbr\u003eStephen D. Golden and Kenneth W. Olsen\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649288753432,"sku":"9780123742780","price":124.39,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123742780.jpg?v=1695013874"},{"product_id":"globins-and-other-nitric-oxide-reactive-proteins-part-a-hardback-9780123742773","title":"Globins and Other Nitric Oxide-Reactive Proteins, Part A (Hardback) 9780123742773","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eGlobins and Other Nitric Oxide-Reactive Proteins, Part A\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eA collection of methods for researchers working in the lab and classroom alike.\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRobert K. Poole (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123742773, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 20 March 2008\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e672 pages, Approx. 110 illustrations\u003cbr\u003e22.9 x 15.1 x 3.6 cm, 1 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThe critically acclaimed laboratory standard for more than forty years, \u003cb\u003eMethods in Enzymology\u003c\/b\u003e is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with over 400 volumes (all of them still in print), the series contains much material still relevant today—truly an essential publication for researchers in all fields of life sciences. \u003cb\u003eMethods in Enzymology\u003c\/b\u003e is now available online at ScienceDirect — full-text online of volumes 1 onwards. For more information about the Elsevier Book Series on ScienceDirect Program, please visit: http:\/\/www.info.sciencedirect.com\/bookseries\/This volume features methods for the study of globin and other nitric oxide-reactive proteins.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSection I.  Nitric Oxide:  Chemical and Analytical Methods\u003cbr\u003e\u003cbr\u003eChapter 1\u003cbr\u003eThe Chemistry of Nitric Oxide and Related Species\u003cbr\u003eMartin H. Hughes\u003cbr\u003e\u003cbr\u003eChapter 2\u003cbr\u003eDelivery of nitric oxide for analysis of the function of cytochrome c’.\u003cbr\u003eLindsay J. Cole, Wilhelmina M. Huston, and James W.B. Moir\u003cbr\u003e\u003cbr\u003eChapter 3\u003cbr\u003eThe preparation and purification of NO gas and the use of NO releasers. The application of NO donors and other agents of nitrosative stress in biological systems  \u003cbr\u003eRubina G. Aga and Martin N. Hughes\u003cbr\u003e\u003cbr\u003eChapter 4\u003cbr\u003eThe Chemistry of Peroxynitrite – Implications for Biological Activity\u003cbr\u003eSara Goldstein and Gabor Merényi\u003cbr\u003e\u003cbr\u003eChapter 5\u003cbr\u003eNitric Oxide (NO) Selective Electrodes\u003cbr\u003eIan R. Davies, Xueji Zhang\u003cbr\u003e\u003cbr\u003eChapter 6\u003cbr\u003eNO, N2O and O2 Reaction Kinetics: Scope and Limitations of the Clark Electrode\u003cbr\u003eL.A.M. Pouvreau, M. J. F. Strampraad, S. Van Berloo, J. H. Kattenberg and S. de Vries\u003cbr\u003e\u003cbr\u003eChapter 7\u003cbr\u003eChemiluminescence quantification of Nitric oxide and its derivatives in liquid samples\u003cbr\u003eJay R. Laver, Tânia M. Stevanin, Robert C. Read\u003cbr\u003e\u003cbr\u003eSection II.  Bacterial and Archaeal  Hemoglobins\u003cbr\u003e\u003cbr\u003eChapter 8\u003cbr\u003eInteractions of nitric oxide with hemoglobin:  from microbes to man\u003cbr\u003eMichael Angelo, Alfred Hausladen and Jonathan S. Stamler\u003cbr\u003e\u003cbr\u003eChapter 9\u003cbr\u003eExpression and purification of E. coli Hmp\u003cbr\u003eRobert K. Poole \u003cbr\u003e\u003cbr\u003eChapter 10\u003cbr\u003eStructural studies on flavohemoglobins\u003cbr\u003eAndrea Ilari and Alberto Boffi\u003cbr\u003e\u003cbr\u003eChapter 11\u003cbr\u003eFlavohemoglobin of Staphylococcus aureus\u003cbr\u003eLígia S. Nobre, Vera L. Gonçalves and Lígia M. Saraiva\u003cbr\u003e\u003cbr\u003eChapter 12\u003cbr\u003eAssay and Characterization of the Nitric Oxide Dioxygenase \tActivity of (Flavo)Hemoglobins\u003cbr\u003ePaul R. Gardner\u003cbr\u003e\u003cbr\u003eChapter 13\u003cbr\u003eGlobin Interactions with Lipids and Membranes\u003cbr\u003eAntonio Di Giulio and Alessandra Bonamore\u003cbr\u003e\u003cbr\u003eChapter 14\u003cbr\u003eAssessment of Biotechnologically Relevant Characteristics of Heterologous Hemoglobins in Escherichia coli\u003cbr\u003ePauli T. Kallio, Christian J. T. Bollinger, Taija Koskenkorva, and Alexander D. Frey\u003cbr\u003e\u003cbr\u003eChapter 15\u003cbr\u003eApplications of the Vitreoscilla hemoglobin (VHb) gene (vgb) for improved microbial fermentation processes\u003cbr\u003eXiao-Xing WEI, Guo-Qiang CHEN\u003cbr\u003e\u003cbr\u003eChapter 16\u003cbr\u003eExpression and Purification of Cgb and Ctb, the NO-Inducible Globins of the Foodborne Bacterial Pathogen Campylobacter jejuni\u003cbr\u003eJames L. Pickford, Laura Wainwright, Guanghui Wu, Robert K. Poole\u003cbr\u003e\u003cbr\u003eChapter 17\u003cbr\u003eMapping Heme-Ligand Tunnel in Group I Truncated(2\/2) Hemoglobins \u003cbr\u003eAlessandra Pesce, Mario Milani, Marco Nardini and Martino Bolognesi\u003cbr\u003e\u003cbr\u003eChapter 18\u003cbr\u003eScavenging of reactive nitrogen species by mycobacterial truncated hemoglobins\u003cbr\u003ePaolo Ascenzi and Paolo Visca\u003cbr\u003e\u003cbr\u003eSection III.  Other Hemoglobins\u003cbr\u003e\u003cbr\u003eChapter 19\u003cbr\u003eExpression, purification and crystallisation of neuro-and cytoglobin\u003cbr\u003eSylvia Dewilde, Kirsten Mees, Laurent Coger, Christophe Lechauve, Michael C. Marden, Alexandra Pesce, Martino Bolognesi, Luc Monees\u003cbr\u003e\u003cbr\u003eChapter 20\u003cbr\u003eMeasurement of distal histidine coordination equilibrium and kinetics in hexacoordinate hemoglobins.\u003cbr\u003eBenoit J. Smagghe, Puspita Halder, and Mark S. Hargrove\u003cbr\u003e\u003cbr\u003eChapter 21\u003cbr\u003ePurification of Class 1 Plant Hemoglobins and Examination of their Functional Properties\u003cbr\u003eAbir U. Igamberdiev and Robert D. Hill\u003cbr\u003e\u003cbr\u003eChapter 22\u003cbr\u003eUse of in silico (computer) methods to predict and analyze the tertiary structure of plant hemoglobins\u003cbr\u003eSabarinathan Kuttalingam Gopalasubramaniam, Verónica Garrocho-Villegas, Genoveva Bustos Rivera, Nina Pastor and Raúl Arredondo-Peter\u003cbr\u003e\u003cbr\u003eChapter 23\u003cbr\u003eA Self-induction Method to Produce High Quantities of Recombinant Functional Flavo-Leghemoglobin Reductase.\u003cbr\u003eEstibaliz Urarte, Iñigo Auzmendi, Selene Rol, Idoia Ariz, Pedro Aparicio-Tejo, Raúl Arredondo-Peter and Jose F. Moran\u003cbr\u003e\u003cbr\u003eChapter 24\u003cbr\u003eSpectroscopic and crystallographic characterization of bis-histidyl adducts in tetrameric hemoglobins\u003cbr\u003eAlessandro Vergara, Luigi Vitagliano, Cinzia Verde, Guido di Prisco, Lelio Mazzarella\u003cbr\u003e\u003cbr\u003eChapter 25\u003cbr\u003eDinitrosyl Iron Complexes Bound with Haemoglobin as Markers of Oxidative Stress\u003cbr\u003eKonstantin B. Shumaev, Olga V. Kosmachevskaya, Alexandr A. Timoshin, Anatoly F. Vanin and Alexey F. Topunov\u003cbr\u003e\u003cbr\u003eChapter 26\u003cbr\u003eLinked analysis of large cooperative, allosteric systems: the case of the giant HBL hemoglobins\u003cbr\u003eNadja Hellmann, Roy E. Weberb and Heinz Decker\u003cbr\u003e\u003cbr\u003eChapter 27\u003cbr\u003eMass Mapping of Large Globin Complexes by Scanning Transmission Electron Microscopy\u003cbr\u003eJoseph S. Wall, Martha N. Simon, Beth Y. Lin, Serge N. Vinogradov\u003cbr\u003e\u003cbr\u003eChapter 28\u003cbr\u003eMini-Hemoglobins from Nemertean Worms\u003cbr\u003eThomas L. Vandergon and Austen F. Riggs\u003cbr\u003e\u003cbr\u003eChapter 29\u003cbr\u003eComparative and Evolutionary Genomics of Globin Genes in Fish\u003cbr\u003eEnrico Negrisolo, Luca Bargelloni, Tomaso Patarnello, Catherine Ozouf-Costaz, Eva Pisano, Guido di Prisco, Cinzia Verde\u003cbr\u003e\u003cbr\u003eChapter 30\u003cbr\u003eInferring Evolution of Fish Proteins:  The Globin Case Study\u003cbr\u003eAgnes Dettai, Guideo de Prisco, Guillaume Lecointre, Elio Parisi, Cinzia Verde\u003cbr\u003e\u003cbr\u003eChapter 31\u003cbr\u003eTracing Globin Phylogeny Using PSI-BLAST Searches \u003cbr\u003eBased on Groups of Sequences \u003cbr\u003eSerge N. Vinogradov\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649289146648,"sku":"9780123742773","price":109.37,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123742773.jpg?v=1695013873"},{"product_id":"structural-genomics-part-a-hardback-9780123744364","title":"Structural Genomics, Part A (Hardback) 9780123744364","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eStructural Genomics, Part A\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThis volume presents step-by-step techniques for researchers that will predict the structure and potential function of proteins by identifying its coding sequence\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eAndrzej Joachimiak (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123744364, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 18 December 2008\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e160 pages\u003cbr\u003e22.9 x 15.1 x 1.8 cm, 0.44 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eStructural genomics is the systematic determination of 3-dimensional structures of proteins representative of the range of protein structure and function found in nature. The goal is to build a body of structural information that will predict the structure and potential function for almost any protein from knowledge of its coding sequence. This is essential information for understanding the functioning of the human proteome, the ensemble of tens of thousands of proteins specified by the human genome.\u003c\/p\u003e  \u003cp\u003eWhile most structural biologists pursue structures of individual proteins or protein groups, specialists in structural genomics pursue structures of proteins on a genome wide scale. This implies large-scale cloning, expression and purification. One main advantage of this approach is economy of scale.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eIntroduction\u003cbr\u003e Analysis of genomes for structural genomics and the limitations of sequence analysis\u003cbr\u003e Structure determination pipeline for structural genomics\u003cbr\u003eGene cloning and protein expression\u003cbr\u003eGene cloning and expression of membrane proteins\u003cbr\u003e High-throughput protein purification for x-ray crystallography and NMR\u003cbr\u003e High-throughput protein crystallization\u003cbr\u003e Structure determination using synchrotron radiation\u003cbr\u003e Application of NMR to structural genomics\u003cbr\u003e Development of key high-throughput technologies: High-throughput functional screening\u003cbr\u003e Development of key high-throughput technologies: Structure prediction and homology modeling\u003cbr\u003e Functional inferences from structure\u003cbr\u003e Structural genomics programs (SARS case)\u003cbr\u003e Structural genomics programs (E.coli)\u003cbr\u003eStructural genomics as a structural foundation for drug discovery\u003cbr\u003e Structural genomics of eukaryote\u003cbr\u003e Structural genomics of complexes\u003cbr\u003e Dissemination structural genomics data to biology community\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], DNA \u0026amp; Genome [\u003ca title=\"See our other books on DNA \u0026amp; Genome\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22DNA%20\u0026amp;%20Genome%20%5BPSAK1%5D%22\"\u003ePSAK1\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649290129688,"sku":"9780123744364","price":114.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123744364.jpg?v=1695013909"},{"product_id":"molecular-biology-of-protein-folding-part-a-hardback-9780123745941","title":"Molecular Biology of Protein Folding, Part A (Hardback) 9780123745941","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eMolecular Biology of Protein Folding, Part A\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eRecent research shows that many unrelated diseases ? Alzheimer's disease, cystic fibrosis, mad cow disease and many forms of cancer ? result from protein folding gone wrong. This volume pulls together compelling and timely reviews to aid researchers in understanding the concepts of protein folding and how protein folding can be monitored and studied.\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eP. Michael Conn (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123745941, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 19 December 2008\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e288 pages\u003cbr\u003e22.9 x 15.1 x 2.3 cm, 0.55 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThe importance of protein folding has been recognized for many years.  It is the underlying etiology in a large number of human diseases and it appears to be a novel method for cellular regulation of the expression of newly translated proteins.  These volumes (Parts A \u0026amp; B) address this important topic.  As a volume in Progress in Nucleic Acid Research and Molecular Biology, this book provides the latest information on the expanding research being conducted on protein folding.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e1. Stability and design of alpha-helical peptides - Andrew Doig\u003cbr\u003e\u003cbr\u003e2. Under-wrapped protein folds in disease and epigenetic change - Ariel Fernandez\u003cbr\u003e\u003cbr\u003e3. Self-organizing dynamics in protein folding - Bernard S. Gerstman\u003cbr\u003e\u003cbr\u003e4. Diffusive models for protein folding - Stephen J Hagen\u003cbr\u003e\u003cbr\u003e5. Toward reliable simulations of protein folding, misfolding and aggregation - Ulrich HE Hansmann\u003cbr\u003e\u003cbr\u003e6. Single-molecule fluorescence studies of protein folding - Gilad Haran\u003cbr\u003e\u003cbr\u003e7. Algorithms for protein folding - Sorin Istrail\u003cbr\u003e\u003cbr\u003e8. Use of protein engineering techniques to elucidate protein folding pathways - Sophie Jackson\u003cbr\u003e\u003cbr\u003e9. The kinetic stabilities of wild-type and disease-associated mutants of aromatic amino acid hydroxylases. Effect of natural chaperone ligand - Aurora Martinez\u003cbr\u003e\u003cbr\u003e10. Chaperone-assisted protein folding in the endoplasmic reticulum - Maurizio Molinari\u003cbr\u003e\u003cbr\u003e11. Protein folding over marginal barriers: ensembles, dynamics and stochastics - Victor Munoz\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Medicine [\u003ca title=\"See our other books on Medicine\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Medicine%20%5BM%5D%22\"\u003eM\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649291997464,"sku":"9780123745941","price":89.57,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123745941.jpg?v=1695013915"},{"product_id":"structural-genomics-part-b-hardback-9780123744425","title":"Structural Genomics, Part B (Hardback) 9780123744425","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eStructural Genomics, Part B\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThis volume presents step-by-step techniques for researchers that will predict the structure and potential function of proteins by identifying its coding sequence\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eAndrzej Joachimiak (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123744425, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 15 December 2009\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e112 pages\u003cbr\u003e22.9 x 15.1 x 1.6 cm, 0.34 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eStructural genomics is the systematic determination of 3-D structures of proteins representative of the range of protein structure and function found in nature. The goal is to build a body of structural information that will predict the structure and potential function for almost any protein from knowledge of its coding sequence. This is essential information for understanding the functioning of the human proteome, the ensemble of tens of thousands of proteins specified by the human genome.\u003c\/p\u003e  \u003cp\u003eWhile most structural biologists pursue structures of individual proteins or protein groups, specialists in structural genomics pursue structures of proteins on a genome wide scale. This implies large-scale cloning, expression and purification. One main advantage of this approach is economy of scale.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eIntroduction\u003cbr\u003e Analysis of genomes for structural genomics and the limitations of sequence analysis\u003cbr\u003e Structure determination pipeline for structural genomics\u003cbr\u003eGene cloning and protein expression\u003cbr\u003eGene cloning and expression of membrane proteins\u003cbr\u003e High-throughput protein purification for x-ray crystallography and NMR\u003cbr\u003e High-throughput protein crystallization\u003cbr\u003e Structure determination using synchrotron radiation\u003cbr\u003e Application of NMR to structural genomics\u003cbr\u003e Development of key high-throughput technologies: High-throughput functional screening\u003cbr\u003e Development of key high-throughput technologies: Structure prediction and homology modeling\u003cbr\u003e Functional inferences from structure\u003cbr\u003e Structural genomics programs (SARS case)\u003cbr\u003e Structural genomics programs (E.coli)\u003cbr\u003eStructural genomics as a structural foundation for drug discovery\u003cbr\u003e Structural genomics of eukaryote\u003cbr\u003e Structural genomics of complexes\u003cbr\u003e Dissemination structural genomics data to biology community\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], DNA \u0026amp; Genome [\u003ca title=\"See our other books on DNA \u0026amp; Genome\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22DNA%20\u0026amp;%20Genome%20%5BPSAK1%5D%22\"\u003ePSAK1\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649292063000,"sku":"9780123744425","price":78.19,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123744425.jpg?v=1695013896"},{"product_id":"guide-to-protein-purification-hardback-9780123745361","title":"Guide to Protein Purification (Hardback) 9780123745361","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eGuide to Protein Purification\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eAn essential reference for any researcher involved in protein purification, this volume is a comprehensive collection of methods necessary for purifying, characterizing, and handling proteins and enzymes\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRichard R Burgess (Edited by), Murray P. Deutscher (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123745361, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 1 December 2009\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e900 pages\u003cbr\u003e22.9 x 15.1 x 4.4 cm, 1.34 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\u003ci\u003eGuide to Protein Purification, Second Edition \u003c\/i\u003eprovides a complete update to existing methods in the field, reflecting the enormous advances made in the last two decades. In particular, proteomics, mass spectrometry, and DNA technology have revolutionized the field since the first edition’s publication but through all of the advancements, the purification of proteins is still an indispensable first step in understanding their function. This volume examines the most reliable, robust methods for researchers in biochemistry, molecular and cell biology, genetics, pharmacology and biotechnology and sets a standard for best practices in the field. It relates how these traditional and new cutting-edge methods connect to the explosive advancements in the field. This \"Guide to\" gives imminently practical advice to avoid costly mistakes in choosing a method and brings in perspective from the premier researchers while presents a comprehensive overview of the field today. \u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e1. Why Purify Enzymes?\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection I: Developing Purification Procedures \u003c\/b\u003e2. Strategies and Considerations for Protein Purifications 3. Use of Bioinformatics in Planning a Protein Purification 4. Preparing A Purification Summary Table\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection II: General Methods for Handling Proteins and Enzymes \u003c\/b\u003e5. Setting Up A Laboratory 6. Buffers: Principle and Practice 7. Measurement of Enzyme Activity 8. Quantitation of Protein 9. Concentration of Proteins and Removal of Solutes 10. Maintaining Protein Stability\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection III: Recombinant Protein Expression and Purification \u003c\/b\u003e11. Selecting an Appropriate Method for Expressing a Recombinant Protein 12. Bacterial Systems for Production of Heterologous Proteins 13. Expression in the Yeast Pichia Pastoris 14. Baculovirus-Insect Cell Expression Systems 15. Recombinant Protein Production By Transient Gene Transfer Into Mammalian Cells 16. Tagging For Protein Expression 17. Refolding of Solubilized Inclusion Body Proteins\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection IV: Preparation of Extracts and Subcellular Fractionation  \u003c\/b\u003e18. Advances In Preparation of Biological Extracts for Protein Purification 19. Isolation of Subcellular Organelles and Structures\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection V: Purification Procedures: Bulk Methods \u003c\/b\u003e20. Protein Precipitation Techniques 21. Affi-Gel Blue for Nucleic Acid Removal and Early Enrichment of Nucleotide Binding Protein\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection VI: Purification Procedures: Chromatographic Methods \u003c\/b\u003e22. Ion Exchange Chromatography 23. Gel Filtration 24. Protein Chromatography on Hydroxyapatite Columns 25. Theory and Use of Hydrophobic Interaction Chromatography in Protein Purification Applications\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection VII: Purification Procedures: Affininty Methods \u003c\/b\u003e26. Affinity Chromatography: General Methods 27. Immobilized-Metal Affinity Chromatography (IMAC) 28. Identification, Production, and Use of Polyol-Responsive Monoclonal Antibodies for Immunoaffinity Chromatography\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection VIII: Purification Procedures: Electrophoretic Methods \u003c\/b\u003e29. One-Dimensional Gel Electrophoresis 30. Protein Analysis Using High-Resolution Two-Dimensional Polyacrylamide Gel Electrophoresis and Isoelectric Focusing 31. Protein Gel Staining Methods: An Introduction And Overview 32. Elution of Proteins From Gels 33. Immunodetection By Protein Blotting Performing and Optimizing Western Blots With An Emphasis on Chemiluminescent Detection\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection IX: Purification Procedures: Membrane Proteins And Glycoproteins \u003c\/b\u003e34. Detergents: An Overview 35. Purification of Membrane Proteins 36. Purification of Recombinant G-Protein-Coupled Receptors 37. Cell-Free Translation Of Integral Membrane Proteins Into Unilamelar Liposomes\u003c\/p\u003e \u003cp\u003e\u003cb\u003eSection X: Characterization of Purified Proteins \u003c\/b\u003e38. Determination of Protein Purity 39. Determination of Size, Molecular Weight, and Presence of Subunits 40. Identification and Quantification of Protein Posttranslational Modifications 41. Parallel Methods For Expression And Purification 42. Techniques To Isolate O2-Sensitive Proteins: [4Fe-4S]-FNR As An Example 43. Rethinking Your Purification Procedure 44. Important But Little Known (Or Forgotten) Artifacts in Protein Biochemistry\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Science: general issues [\u003ca title=\"See our other books on Science: general issues\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Science:%20general%20issues%20%5BPD%5D%22\"\u003ePD\u003c\/a\u003e], Pharmacology [\u003ca title=\"See our other books on Pharmacology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Pharmacology%20%5BMMG%5D%22\"\u003eMMG\u003c\/a\u003e], Immunology [\u003ca title=\"See our other books on Immunology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Immunology%20%5BMJCM%5D%22\"\u003eMJCM\u003c\/a\u003e], Pre-clinical medicine: basic sciences [\u003ca title=\"See our other books on Pre-clinical medicine: basic sciences\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Pre-clinical%20medicine:%20basic%20sciences%20%5BMF%5D%22\"\u003eMF\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649292128536,"sku":"9780123745361","price":118.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123745361_38ee17cf-6bfd-4b08-8cc5-bafd4d714e75.jpg?v=1695013908"},{"product_id":"molecular-biology-of-protein-folding-part-b-hardback-9780123745958","title":"Molecular Biology of Protein Folding, Part B (Hardback) 9780123745958","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eMolecular Biology of Protein Folding, Part B\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eCompelling and timely reviews to aid researchers in understanding the concepts of protein folding which when goes wrong causes many unrelated diseases such as Alzheimer's disease and cystic fibrosis\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eP. Michael Conn (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123745958, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 8 December 2008\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e288 pages\u003cbr\u003e22.9 x 15.1 x 2.3 cm, 0.53 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eNucleic acids are the fundamental building blocks of DNA and RNA and are found in virtually every living cell. Molecular biology is a branch of science that studies the physicochemical properties of molecules in a cell, including nucleic acids, proteins, and enzymes. Increased understanding of nucleic acids and their role in molecular biology will further many of the biological sciences including genetics, biochemistry, and cell biology. Progress in Nucleic Acid Research and Molecular Biology is intended to bring to light the most recent advances in these overlapping disciplines with a timely compilation of reviews comprising each volume.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e1. Stability and design of alpha-helical peptides - Andrew Doig\u003cbr\u003e\u003cbr\u003e2. Under-wrapped protein folds in disease and epigenetic change - Ariel Fernandez\u003cbr\u003e\u003cbr\u003e3. Self-organizing dynamics in protein folding - Bernard S. Gerstman\u003cbr\u003e\u003cbr\u003e4. Diffusive models for protein folding - Stephen J Hagen\u003cbr\u003e\u003cbr\u003e5. Toward reliable simulations of protein folding, misfolding and aggregation - Ulrich HE\tHansmann\u003cbr\u003e\u003cbr\u003e6. Single-molecule fluorescence studies of protein folding - Gilad Haran\u003cbr\u003e\u003cbr\u003e7. Algorithms for protein folding - Sorin Istrail\u003cbr\u003e\u003cbr\u003e8. Use of protein engineering techniques to elucidate protein folding pathways - Sophie Jackson\u003cbr\u003e\u003cbr\u003e9. The kinetic stabilities of wild-type and disease-associated mutants of aromatic amino acid hydroxylases. Effect of natural chaperone ligand - Aurora Martinez\u003cbr\u003e\u003cbr\u003e10. Chaperone-assisted protein folding in the endoplasmic reticulum - Maurizio Molinari\u003cbr\u003e\u003cbr\u003e11. Protein folding over marginal barriers: ensembles, dynamics and stochastics - Victor Munoz\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649293701400,"sku":"9780123745958","price":131.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123745958.jpg?v=1695013913"},{"product_id":"molecular-biology-of-rgs-proteins-hardback-9780123747594","title":"Molecular Biology of RGS Proteins (Hardback) 9780123747594","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eMolecular Biology of RGS Proteins\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eRory A. Fisher (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123747594, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 18 September 2009\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e508 pages\u003cbr\u003e22.9 x 15.1 x 3 cm, 0.65 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003ci\u003eMolecular Biology of RGS Proteins\u003c\/i\u003e, a volume of \u003ci\u003eProgress in Molecular Biology and Translational Science\u003c\/i\u003e, will include historical discussion of RGS proteins, the role of RGS proteins in addiction, depression and Parkinson's disease and the biology and functional regulation of RGS9 isoforms. This publication further discusses RGS proteins in cellular signaling, protein control in lymphocyte function, and alternative splicing of RGS transcripts and nuclear RGS proteins, offering the latest in research of RGS proteins.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e1. RGS proteins: the early days\t\u003cbr\u003eHenrik Dohlman\u003cbr\u003e\u003cbr\u003e2. The role of RGS proteins in addiction, depression and Parkinsons disease\t\u003cbr\u003eVanna Zachariou\u003cbr\u003e\u003cbr\u003e3. Biology and functional regulation of RGS9 isoforms\t\u003cbr\u003eKirill Martemyanov\u003cbr\u003e\u003cbr\u003e4. RGS protein function in C. elegans\t\u003cbr\u003eMichael Koelle \u003cbr\u003e\u003cbr\u003e5.G Beta 5 in the visual system\u003cbr\u003eJason Chen \u003cbr\u003e\u003cbr\u003e6. Roles of RGS proteins and RGS homology domains in signaling\t\u003cbr\u003eJohn Tesmer\u003cbr\u003e\u003cbr\u003e7.Gb5-RGS protein complexes\t\u003cbr\u003eVladlen Slepak\u003cbr\u003e\u003cbr\u003e8. Multifunctional roles of RGS Proteins in cellular signaling\t\u003cbr\u003eJohn Hepler \u003cbr\u003e\u003cbr\u003e9. RGS protein control of lymphocyte function\u003cbr\u003eJohn Kehrl\u003cbr\u003e\u003cbr\u003e10. RGS-insensitive G proteins to study endogenous RGS protein function\t\u003cbr\u003eRichard Neubig \u003cbr\u003e\u003cbr\u003e11. Alternative splicing of RGS transcripts and nuclear RGS proteins\t\u003cbr\u003eRory Fisher\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649298125080,"sku":"9780123747594","price":89.57,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123747594.jpg?v=1695013940"},{"product_id":"advances-in-protein-chemistry-and-structural-biology-hardback-9780123748270","title":"Advances in Protein Chemistry and Structural Biology (Hardback) 9780123748270","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eAdvances in Protein Chemistry and Structural Biology\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eA new eclectic volume that will serve as an essential resource for protein chemists\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eDavid S. Eisenberg (Edited by), Alexander McPherson (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123748270, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 23 December 2009\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e184 pages\u003cbr\u003e22.9 x 15.1 x 1.9 cm, 0.46 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\"The authority, originality, and editing of the reviews are first class.\" \u003cbr\u003e\u003cb\u003e-- NATURE\u003c\/b\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003ePublished continuously since 1944, the \u003ci\u003eAdvances in Protein Chemistry and Structural Biology\u003c\/i\u003e serial has been a continuous, essential resource for protein chemists. Covering reviews of methodology and research in all aspects of protein chemistry, including purification\/expression, proteomics, modeling and structural determination and design, each volume brings forth new information about protocols and analysis of proteins while presenting the most recent findings from leading experts in a broad range of protein-related topics. This eclectic volume features articles on a variety of topical subjects.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e1. Angiopoietins and Tie Receptors (Nikolov)\u003cbr\u003e2. Tandem repeats in proteins: sequence, structure and function (Kajava)\u003cbr\u003e3. Protein aggregation: from inclusion bodies to amyloid and biomaterials (Mitraki)\u003cbr\u003e4. Modeling and structural determination and design (Morozov)\u003cbr\u003e5. Structure and role of periplasmic chaperones involved in bacterial secretion (Waksman)\u003cbr\u003e6. Structural bases for corneal transparency (Knupp)\u003cbr\u003e7. Taking charge of proteins: the simple side of intermolecular electrostatics and protein aggregation (Faull)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649299861784,"sku":"9780123748270","price":85.66,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123748270.jpg?v=1695013943"},{"product_id":"membrane-protein-crystallization-hardback-9780123749871","title":"Membrane Protein Crystallization (Hardback) 9780123749871","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eMembrane Protein Crystallization\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eLarry DeLucas (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123749871, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 1 October 2009\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e336 pages, 53 illustrations (23 in full color)\u003cbr\u003e22.9 x 15.1 x 2.4 cm, 0.57 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThis volume of Current Topics in Membranes focuses on Membrane Protein Crystallization, beginning with a review of past successes and general trends, then further discussing challenges of mebranes protein crystallization, cell free production of membrane proteins and novel lipids for membrane protein crystallization.  This publication also includes tools to enchance membrane protein crystallization, technique advancements, and crystallization strategies used for photosystem I and its complexes, establishing Membrane Protein Crystallization as a needed, practical reference for researchers.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eIntroduction: Review of past successes and general trends in membrane protein crystallization\u003cbr\u003eLarry DeLucas \u003cbr\u003e\u003cbr\u003e\u003cbr\u003eChapter 1:  “Introduction to the Crystallization of Biological Macromolecules?, Alex MacPherson\u003cbr\u003e\u003cbr\u003eChapter 2:  “Challenges of Membrane Protein Crystallization?\u003cbr\u003eMichael Wiener\u003cbr\u003e\u003cbr\u003eChapter 3: “Cell Free Production of Membrane Proteins?, \u003cbr\u003eVolker Erdmann, Michael Kubick1, Helmut Merk1, \u003cbr\u003eWolfgang Stiege1 and Jan Strey1    \u003cbr\u003e\u003cbr\u003eChapter 4:  “In Vitro Synthesis of Post-translationally Modified Membrane Proteins?, \u003cbr\u003eVolker Erdmann,Michael Kubick1, Helmut Merk1, and Wolfgang Stiege1\u003cbr\u003e\u003cbr\u003eChapter 5:  “Novel Rhodobactar Membrane Protein Expression Factory?\u003cbr\u003ePhilip Laible and Deborah K. Hanson\u003cbr\u003e\u003cbr\u003eChapter 6:   \"Detergent selection and optimization in membrane protein crystallization\"\u003cbr\u003eTina Iverson\u003cbr\u003e\u003cbr\u003eChapter 7:  “Novel Lipids for Membrane Protein Crystallization?\u003cbr\u003eMartin Caffrey\u003cbr\u003e\u003cbr\u003eChapter 8:  “Bicelle Membrane Protein Crystallization?\u003cbr\u003eJames Bowie\u003cbr\u003e\u003cbr\u003eChapter 9:   “Novel Approaches for Membrane Protein Crystallization?\u003cbr\u003eWilliam Cogdell\u003cbr\u003e\u003cbr\u003eChapter 10:   “Tools to Enhance Membrane Protein Crystallization?\u003cbr\u003eWilliam Wilson Charles Henry and Larry DeLucas\u003cbr\u003e\u003cbr\u003eChapter 11:   “Advances in Microfluidic Membrane Protein Crystallization Techniques?, Peter Nollert and Cory Gerdts\u003cbr\u003e\u003cbr\u003eChapter 12: “Crystallization Strategies Used for Photosystem I and its Complexes?\u003cbr\u003ePetra Fromme\u003cbr\u003e\u003cbr\u003eChapter 13: “â-barrel Membrane Protein Crystallization?\u003cbr\u003eMikio Tanabe and Tina Iverson\u003cbr\u003e\u003cbr\u003eChapter 14: “Membrane Proteins: the New Soluble Proteins?\u003cbr\u003eJames Naismith\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649304875288,"sku":"9780123749871","price":131.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123749871_d463074b-98b0-44c2-8b5a-a7123406030b.jpg?v=1695013961"},{"product_id":"structure-and-function-of-calcium-release-channels-hardback-9780123810373","title":"Structure and Function of Calcium Release Channels (Hardback) 9780123810373","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eStructure and Function of Calcium Release Channels\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cfont size=\"4\"\u003eIrina Serysheva (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123810373, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 22 September 2010\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e372 pages, 53 illustrations (23 in full color)\u003cbr\u003e22.9 x 15.1 x 2.5 cm, 0.66 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThis volume of Current Topics in Membranes focuses on Membrane Protein Crystallization, beginning with a review of past successes and general trends, then further discussing challenges of mebranes protein crystallization, cell free production of membrane proteins and novel lipids for membrane protein crystallization.  \u003cbr\u003e\u003cbr\u003eThis publication also includes tools to enchance membrane protein crystallization, technique advancements, and crystallization strategies used for photosystem I and its complexes, establishing Membrane Protein Crystallization as a needed, practical reference for researchers.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003ePART 1: RyR Ca\u003csup\u003e2+\u003c\/sup\u003e Release channels\u003c\/p\u003e \u003col\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRyRs: their disposition, frequency and relationships with other proteins of calcium release units (Clara Franzini Armstrong).\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eElectron Microscopy of Ryanodine Receptors (Terrence Wagenknecht and Zheng Li).\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eThe ryanodine receptor pore: is there a consensus view? (Carney, J; Mason, SA; Viero, CL and Williams, AJ)\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRegulation of the RyR channel gating by different modulators (Derek Laver).\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRegulation of Ryanodine Receptor Ion Channels through Post-translational Modifications. (Gerhard Meissner).\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eCrosstalk via the sarcoplasmic gap: The DHPR - RyR interaction (Manfred Grabner and Anamika Dayal).\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRyanodinopathies: RyR-linked Muscle Diseases (Lan Wei and Robert T. Dirksen).\u003c\/li\u003e \u003cp\u003ePART 2: IP\u003csub\u003e3\u003c\/sub\u003eR Ca\u003csup\u003e2+\u003c\/sup\u003e Release channels\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eStructure of IP\u003csub\u003e3\u003c\/sub\u003e Receptors. (Irina I. Serysheva and Steven J. Ludtke)\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMolecular Architecture Of The Inositol 1,4,5-trisphosphate Receptor Pore. (Darren Boehninng)\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdenophostins: high-affinity agonists of IP\u003csub\u003e3\u003c\/sub\u003e receptors. (Ana M. Rossi, Andrew, M. Riley, Barry V. L. Potter and Colin W. Taylor)\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRegulation of IP\u003csub\u003e3\u003c\/sub\u003eR channel gating by Ca\u003csup\u003e2+\u003c\/sup\u003e and Ca\u003csup\u003e2+\u003c\/sup\u003e Binding Proteins (J. Kevin Foskett\u003csup\u003e \u003c\/sup\u003eand Don-On Daniel Mak).\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRegulation of IP\u003csub\u003e3\u003c\/sub\u003eR channels through phosphorylation\/ATP (Matthew J. Betzenhauser and David I. Yule).\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRole of thiols in the structure and function of Inositol trisphosphate receptors (Suresh Joseph).\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eInositol 1,4,5-tripshosphate receptor, calcium signaling and polyglutamine expansion disorders (Ilya Bezprozvanny).\u003c\/li\u003e \u003c\/ol\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Animal physiology [\u003ca title=\"See our other books on Animal physiology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Animal%20physiology%20%5BPSVD%5D%22\"\u003ePSVD\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Physiology [\u003ca title=\"See our other books on Physiology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Physiology%20%5BMFG%5D%22\"\u003eMFG\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649308479768,"sku":"9780123810373","price":138.89,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123810373_6c8f9044-90f2-4a32-947c-1953929888fe.jpg?v=1695014001"},{"product_id":"protein-structure-and-diseases-hardback-9780123812629","title":"Protein Structure and Diseases (Hardback) 9780123812629","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProtein Structure and Diseases\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThis volume presents step-by-step techniques for researchers that will predict the structure and potential function of proteins by identifying its coding sequence\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRossen Donev (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123812629, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 12 July 2011\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e312 pages\u003cbr\u003e22.9 x 15.1 x 2.3 cm, 0.66 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eStructural genomics is the systematic determination of 3D structures of proteins representative of the range of protein structure and function found in nature. The goal is to build a body of structural information that will predict the structure and potential function for almost any protein from knowledge of its coding sequence. This is essential information for understanding the functioning of the human proteome, the ensemble of tens of thousands of proteins specified by the human genome.\u003c\/p\u003e  \u003cp\u003eWhile most structural biologists pursue structures of individual proteins or protein groups, specialists in structural genomics pursue structures of proteins on a genome wide scale. This implies large-scale cloning, expression and purification. One main advantage of this approach is economy of scale.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003col\u003e \u003cli\u003eGraphical representation and mathematical characterization of protein sequences and applications to viral proteinsAmbarnil Ghosh and Ashesh Nandy\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eStructural, thermodynamic and mechanistical studies in uroporphyrinogen III synthase. Molecular basis of congenital erythropoietic porphyriaArola Fortian, David Castaño, Esperanza Gonzalez, Ana Laín, Juan M. Falcon-Perez and Oscar Millet\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRole of Fibrin Structure in Thrombosis and Vascular DiseaseAmy L. Cilia La Corte, Helen Philippou and Robert A. S. Ariëns\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eStructural, Dynamic, and Functional Aspects of Helix Association in Membranes: a Computational ViewAnton A. Polyansky, Pavel E. Volynsky, Roman G. Efremov\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eProteins MOVE! Protein dynamics and long-range allostery in cell signalingZimei Bu and David J. E. Callaway\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eStructural diversity of class I MHC like molecules and its implications in binding specificitiesMd. Imtaiyaz Hassan and Faizan Ahmad\u003c\/li\u003e\n\u003c\/ol\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], DNA \u0026amp; Genome [\u003ca title=\"See our other books on DNA \u0026amp; Genome\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22DNA%20\u0026amp;%20Genome%20%5BPSAK1%5D%22\"\u003ePSAK1\u003c\/a\u003e], Pharmacology [\u003ca title=\"See our other books on Pharmacology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Pharmacology%20%5BMMG%5D%22\"\u003eMMG\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649308938520,"sku":"9780123812629","price":110.86,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123812629.jpg?v=1695014006"},{"product_id":"protein-prenylation-part-a-hardback-9780123813398","title":"Protein Prenylation, Part A (Hardback) 9780123813398","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProtein Prenylation, Part A\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eCutting edge reviews\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eChristine Hrycyna (Volume editor), Martin Bergo (Volume editor), Fuyuhiko Tamanoi (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123813398, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 2 September 2011\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e356 pages\u003cbr\u003e22.9 x 15.1 x 2.5 cm, 0.64 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThis volume of \u003ci\u003eThe Enzymes\u003c\/i\u003e features high-caliber thematic articles on the topic of glycosylphosphatidylinositol (GPI) anchoring of proteins.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eChapter 1: Protein prenylation: A perspective on initial discoveries\u003c\/p\u003e \u003cp\u003eJohn Glomset\u003c\/p\u003e \u003cp\u003eChapter 2: Insights into the function of prenylation from nuclear lamin farnesylation\u003c\/p\u003e \u003cp\u003eMichael Sinensky\u003c\/p\u003e \u003cp\u003eChapter 3: Posttranslational Processing of Nuclear Lamins \u003c\/p\u003e \u003cp\u003eBrandon S. J. Davies, Catherine Coffinier, Shao H. Yang, Hea-Jin Jung, Loren G. Fong, and Stephen G. Young\u003c\/p\u003e \u003cp\u003eChapter 4: Prenylated Proteins in Peroxisome Biogenesis\u003c\/p\u003e \u003cp\u003eRobert Rucktäschel, Rezeda Mirgalieva, Ralf Erdmann\u003c\/p\u003e \u003cp\u003eChapter 5: Lipid Modification of Ras Superfamily GTPases: Not Just Membrane Glue\u003c\/p\u003e \u003cp\u003eEmily J. Chenette,\u003csup\u003e, \u003c\/sup\u003eChanning J. Der\u003c\/p\u003e \u003cp\u003eChapter 6: Heterogeneous Prenyl Processing of the Heterotrimeric G protein Gamma Subunits\u003c\/p\u003e \u003cp\u003eJohn Hildebrandt\u003c\/p\u003e \u003cp\u003eChapter 7: Farnesylation versus geranylgeranylation in G-protein-mediated light signaling \u003c\/p\u003e \u003cp\u003eMasahiro Okada , Hidetoshi Kassai, Yoshitaka Fukada\u003c\/p\u003e \u003cp\u003eChapter 8: Organization and function of the Rab prenylation and recycling machinery\u003c\/p\u003e \u003cp\u003eKirill Alexandrov, Yaowen Wu, Wulf Blankenfeldt, Herbert Waldmann, Roger S. Goody\u003csup\u003e \u003c\/sup\u003e\u003c\/p\u003e \u003cp\u003eChapter 9: Protein prenylation and CaaX processing in plants\u003c\/p\u003e \u003cp\u003eShaul Yalovsky\u003c\/p\u003e \u003cp\u003eChapter 10: Posttranslational isoprenylation on tryptophan residue in Bacillus subtilis\u003c\/p\u003e \u003cp\u003eMasahiro Okada, Fumitada Tsuji, Youji Sakagami\u003c\/p\u003e \u003cp\u003eChapter 11: Global analysis of prenylated proteins by the use of a tagging via substrate approach\u003c\/p\u003e \u003cp\u003eLai N. Chan, Fuyuhiko Tamanoi\u003c\/p\u003e \u003cp\u003eChapter 12: Global Identification of Protein Prenyltransferase Substrates: Defining the Prenylated Proteome\u003c\/p\u003e \u003cp\u003eCorissa L. Lamphear, Elaina A. Zverina, James L. Hougland, Carol A. Fierke\u003c\/p\u003e \u003cp\u003eChapter 13: Structural biochemistry of CaaX protein prenyltransferases\u003c\/p\u003e \u003cp\u003eMichael A. Hast , Lorena S. Beese\u003c\/p\u003e \u003cp\u003eChapter 14: Genetic Analyses of the CAAX Protein Prenyltransferases in Mice\u003c\/p\u003e \u003cp\u003eMOHAMED X. IBRAHIM, OMAR M. KHAN, MARTIN O. BERGO\u003c\/p\u003e \u003cp\u003eChapter 15: Farnesyl Transferase Inhibitors: From Targeted Cancer Therapeutic to a Potential Treatment for Progeria\u003c\/p\u003e \u003cp\u003eW. Robert Bishop, Ronald Doll, Paul Kirschmeier \u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649311723800,"sku":"9780123813398","price":110.19,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123813398.jpg?v=1695014023"},{"product_id":"advances-in-protein-chemistry-and-structural-biology-hardback-9780123812643","title":"Advances in Protein Chemistry and Structural Biology (Hardback) 9780123812643","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eAdvances in Protein Chemistry and Structural Biology\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThis volume presents step-by-step techniques for researchers that will predict the structure and potential function of proteins by identifying its coding sequence\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eRossen Donev (Series edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123812643, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 16 December 2010\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e296 pages\u003cbr\u003e22.9 x 15.1 x 2.3 cm, 0.62 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eStructural genomics is the systematic determination of 3-D structures of proteins representative of the range of protein structure and function found in nature. The goal is to build a body of structural information that will predict the structure and potential function for almost any protein from knowledge of its coding sequence. This is essential information for understanding the functioning of the human proteome, the ensemble of tens of thousands of proteins specified by the human genome.\u003c\/p\u003e  \u003cp\u003eWhile most structural biologists pursue structures of individual proteins or protein groups, specialists in structural genomics pursue structures of proteins on a genome wide scale. This implies large-scale cloning, expression and purification. One main advantage of this approach is economy of scale.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003col\u003e \u003cli\u003eProteomics technologies for the global identification and quantification of proteins\u003c\/li\u003e \u003cp\u003eIan A. Brewis and P. Brennan\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eTargeted metabolomics and mass spectrometry \u003c\/li\u003e \u003cp\u003eE. Dudley, M. Yousef, Y. Wang, W.J. Griffiths \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMechanisms of Protein Circular Dichroism: Insights from Computational Modelling\u003c\/li\u003e \u003cp\u003eTatyana Karabencheva and Christo Christov\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eFine architecture and mutation mapping of human brain inhibitory system ligand gated ion channels by high-throughput homology modeling\u003c\/li\u003e \u003cp\u003eJonathan G. L. Mullins, Seo-Kyung Chung and Mark I. Rees\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003ePositive and Negative Modulation of Nicotinic Receptors\u003c\/li\u003e \u003cp\u003eHugo R. Arias\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eSonochemically Born Proteinaceous Micro- and Nanocapsules\u003c\/li\u003e \u003c\/ol\u003e \u003cp\u003eElena D. Vassileva and Neli S. Koseva\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], DNA \u0026amp; Genome [\u003ca title=\"See our other books on DNA \u0026amp; Genome\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22DNA%20\u0026amp;%20Genome%20%5BPSAK1%5D%22\"\u003ePSAK1\u003c\/a\u003e], Organic chemistry [\u003ca title=\"See our other books on Organic chemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Organic%20chemistry%20%5BPNN%5D%22\"\u003ePNN\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649313067288,"sku":"9780123812643","price":124.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123812643.jpg?v=1695014005"},{"product_id":"constitutive-activity-in-receptors-and-other-proteins-part-a-hardback-9780123812988","title":"Constitutive Activity in Receptors and Other Proteins, Part A (Hardback) 9780123812988","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eConstitutive Activity in Receptors and Other Proteins, Part A\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cp\u003eThis volume of Methods in Enzymology covers the current methodology for the detection and assessment of constitutively active proteins. \u003c\/p\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eMelvin I. Simon (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123812988, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 26 November 2010\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e804 pages\u003cbr\u003e22.9 x 15.1 x 4 cm, 1.22 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eThis volume of \u003ci\u003eMethods in Enzymology\u003c\/i\u003e covers the current methodology for the detection and assessment of constitutively active proteins. The chapters written by expert authors who are leaders in the field, provide hints and tricks not available in primary research publications.It is extensively referenced, with useful figures and tables throughout the volume.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eSection I-- Identification and Measurement of Constitutive Activity\u003c\/p\u003e \u003col\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutive activity at the cannabinoid CB\u003csub\u003e1\u003c\/sub\u003e receptor and behavioral responses \u003c\/li\u003e \u003cp\u003eKatherine E. Hanlon and Todd W. Vanderah\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eDetecting constitutive activity and protean agonism at the cannabinoid-2 receptor. \u003c\/li\u003e \u003cp\u003eMassimiliano Beltramo, Rossella Brusa, Isabella Mancini, Paola Scandroglio, Massimiliano. Beltramo\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eModulation of constitutive activity of the ghrelin receptor by use of pharmacological tools as well as mutagenesis \u003c\/li\u003e \u003cp\u003eBirgitte Holst and Jacek Mokrosinski \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAssessment of constitutive activity and internalization of GPR54 (Kiss1-r). \u003c\/li\u003e \u003cp\u003eMacarena Pampillo and Andy Videsh Babwah\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAssessment of Constitutive Activity in EP Prostanoid Receptors \u003c\/li\u003e \u003cp\u003eHiromichi Fujino, Toshihiko Murayama, and John W. Regan\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003ea\u003csub\u003e1D\u003c\/sub\u003e-Adrenergic receptors: constitutive activity and reduced expression at the plasma membrane\u003c\/li\u003e \u003cp\u003eJ Adolfo Garcia-Sáinz, M. Teresa Romero-Ávila and Luz del Carmen Medina\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutive activity of the histamine H\u003csub\u003e1\u003c\/sub\u003e receptor\u003c\/li\u003e \u003cp\u003eSaskia Nijmeijer, Rob Leurs and Henry F Vischer\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutive activity of somatostatin receptor subtypes\u003c\/li\u003e \u003cp\u003eAnat Ben-Shlomo, Kolja Wawrowsky and Shlomo Melmed\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAssessment of homologous internalization of constitutively active N111G mutant of AT\u003csub\u003e1\u003c\/sub\u003e receptor\u003c\/li\u003e \u003cp\u003eMohiuddin Ahmed Bhuiyan and Takafumi Nagatomo\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMethods to detect cell surface expression and constitutive activity of GPR6\u003c\/li\u003e \u003cp\u003eBalakrishna M. Prasad, Bettye Hollins and Nevin A. Lambert\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eß\u003csub\u003e3\u003c\/sub\u003e-adrenoceptor agonists and (antagonists as) inverse agonists: history, perspective, constitutive activity and stereospecific binding. \u003c\/li\u003e \u003cp\u003eMaria Grazia Perrone and Antonio Scilimati\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutive Activity of the Lutropin Receptor and its Allosteric Modulation by Receptor Heterodimerization\u003c\/li\u003e \u003cp\u003eDeborah L. Segaloff\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAssessing Constitutive Activity of Extracellular Calcium-Sensing Receptors in Vitro and in Bone\u003c\/li\u003e \u003cp\u003eWenhan Chang, Melita Dvorak, and Dolores Shoback\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutive Activity of Neural Melanocortin Receptors. \u003c\/li\u003e \u003cp\u003eYa-Xiong Tao, Hui Huang, Zhi-Qiang Wang, Fan Yang, Jessica N. Williams, and Gregory V. Nikiforovich\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMeasurement of Constitutive Activity of BMP Type I receptors \u003c\/li\u003e \u003cp\u003ePeter ten Dijke\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eProbing the CA among dopamine D1 and D5 receptors and their mutants\u003c\/li\u003e \u003cp\u003eBianca Plouffe, Jean-Philippe D’Aoust, Vincent Laquerre, Binhui Liang and Mario Tiberi\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eIdentification of Gain-of-Function Variants of the Human Prolactin Receptor\u003c\/li\u003e \u003cp\u003eVincent Goffin, Roman L. Bogorad, and Philippe Touraine\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eInvestigations of Activated ACVR1\/ALK2, a Bone Morphogenetic Protein (BMP) Type I Receptor that Causes Fibrodysplasia Ossificans Progressiva \u003c\/li\u003e \u003cp\u003eFrederick. Kaplan, Petra Seemann, Julia Haupt, Meiqi Xu, Vitali Lounev, Mary Mullins, Eileen M. Shore\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eIdentification and evaluation of constitutively active thyroid stimulating hormone receptor mutations\u003c\/li\u003e \u003cp\u003eJoaquin Lado-Abeal, Leah R. Quisenberry, and Isabel Castro-Piedras\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAssessment of constitutive activity of a G protein-coupled receptor, Cpr2, in Cryptococcus neoformans by heterologous and homologous methods \u003c\/li\u003e \u003cp\u003eChaoyang Xue, Yina Wang, and Yen-Ping Hsueh\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eIn vitro and in vivo assessment of mu opioid receptor constitutive activity. \u003c\/li\u003e \u003cp\u003eEdward J. Bilsky, Denise Giuvelis, Melissa D. Osborn, Christina M. Dersch, Heng Xu and Richard B. Rothman\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutively active µ-opioid methods\u003c\/li\u003e \u003cp\u003eMark. Connor and John Traynor\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eProtein Kinase Ck2 is a Constitutively-Active Enzyme That Promotes Cell Survival: Strategies To Identify Ck2 Substrates and Manipulate Its Activity In Mammalian Cells \u003c\/li\u003e \u003cp\u003eJacob P. Turowec, James S. Duncan, Ashley C. French, Laszlo Gyenis, Nicole A. St. Denis, Greg J. Vilk, and David W. Litchfield \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAssessment of Ck2 Constitutive Activity In Cancer Cells\u003c\/li\u003e \u003cp\u003eMaria Ruzzene, Giovanni Di Maira, Kendra Tosoni, and Lorenzo A. Pinna\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eStructural basis of the constitutive activity of protein kinase CK2\u003c\/li\u003e \u003cp\u003eBirgitte B. Olsen, Barbara Guerra, Karsten Niefind and Olar-Georg Issinger font error\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMeasuring the Constitutive Activation of c-Jun N-terminal Kinase Isoforms\u003c\/li\u003e \u003cp\u003eRyan T. Nitta, Shawn S. Badal, and Albert J. Wong\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMeasurement of constitutive MAPK and PI3K\/AKT signaling activity in human cancer cell lines.\u003c\/li\u003e \u003cp\u003eKeiran S.M. Smalley\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutive activity of GPR40\/FFA1: Intrinsic or assay dependent?\u003c\/li\u003e \u003cp\u003eLeigh A Stoddart\u003csup\u003e \u003c\/sup\u003eand Graeme Milligan\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutive activity of TRP channels: methods for measuring the activity and its outcome\u003c\/li\u003e \u003cp\u003eBaruch Minke\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMeasurement of Orexin (Hypocretin) and Substance P Effects On Constitutively Active Inward Rectifier K+ Channels in Brain Neurons\u003c\/li\u003e \u003cp\u003eYasuko Nakajima and Shigehiro Nakajima\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eCharacterization of G protein receptor kinase 4 and measuring its constitutive activity in vivo\u003c\/li\u003e \u003cp\u003eBradley T. Andresen\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eVoltage-clamp based methods for the detection of constitutively active acetylcholine-gated I\u003csub\u003eK,ACh \u003c\/sub\u003echannels in the diseased heart \u003c\/li\u003e \u003cp\u003eNiels Voigt, Samy Makary, Stanley Nattel, Dobromir Dobrev\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAssaying Wave and WASH complex constitutive activities towards the Arp2\/3 complex. \u003c\/li\u003e \u003c\/ol\u003e \u003cp\u003eEmmanuel DERIVERY and Alexis GAUTREAU \u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649313493272,"sku":"9780123812988","price":132.98,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123812988.jpg?v=1695013997"},{"product_id":"constitutive-activity-in-receptors-and-other-proteins-part-b-hardback-9780123812964","title":"Constitutive Activity in Receptors and Other Proteins, Part B (Hardback) 9780123812964","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eConstitutive Activity in Receptors and Other Proteins, Part B\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cp\u003eThis volume of Methods in Enzymology covers the current methodology for the detection and assessment of constitutively active proteins. \u003c\/p\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eMelvin I. Simon (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123812964, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 24 November 2010\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e708 pages\u003cbr\u003e22.9 x 15.1 x 3.7 cm, 1.1 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eThis volume of \u003ci\u003eMethods in Enzymology\u003c\/i\u003e covers the current methodology for the detection and assessment of constitutively active proteins. The chapters written by expert authors who are leaders in the field, provide hints and tricks not available in primary research publications.It is extensively referenced, with useful figures and tables throughout the volume.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003col\u003e \u003col\u003e \u003cli\u003eIdentification and characterization of Steroidogenic Factor-1 inverse agonists. \u003c\/li\u003e \u003cp\u003eMabrouka Doghman, Franck Madoux, Peter Hodder, and Enzo Lalli\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAssessment of inverse agonism for the angiotensin II type 1 receptor\u003c\/li\u003e \u003cp\u003eHiroshi Akazawa, Noritaka Yasuda, Shin-ichiro Miura, Issei Komuro\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMeasurement of inverse agonism in BARs\u003c\/li\u003e \u003cp\u003eCarlos Alberto Taira\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eInverse agonism of antidepressants: in vitro and in vivo studies\u003c\/li\u003e \u003cp\u003eJoel Bockaert\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eDifferential inverse agonism at the human muscarinic M\u003csub\u003e3\u003c\/sub\u003e receptor\u003c\/li\u003e \u003cp\u003ePaola Casarosa\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eGhrelin Receptor: High Constitutive Activity and Methods for Developing Inverse Agonists.\u003c\/li\u003e \u003cp\u003eConstance Chollet\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutive activity and inverse agonism at the a1a and a1b adrenergic receptor subtypes.\u003c\/li\u003e \u003cp\u003eSusanna. Cotecchia\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMeasurement of inverse agonism of the cannabinoid receptor\u003c\/li\u003e \u003cp\u003eTung Fong\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eConstitutively Active Thyrotropin (TSH) and Thyrotropin-Releasing Hormone (TRH) Receptors and Their Inverse Agonists\u003c\/li\u003e \u003cp\u003eMarvin C. Gershengorn\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eInverse retinoid agonists and neutral antagonists\u003c\/li\u003e \u003cp\u003eHinrich Gronemeyer\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003e?-Aminobutyric Acid Type A (GABA\u003csub\u003eA\u003c\/sub\u003e) Receptor Subtype Inverse Agonists as Therapeutic Agents in Cognition \u003c\/li\u003e \u003cp\u003eGabriella Guerrini and Ciciani Giovanna\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAssays for inverse agonists in the visual system.\u003c\/li\u003e \u003cp\u003eMasahiro Kono\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eReceptor-driven identification of novel human A3 adenosine receptor antagonists as potential therapeutic agents\u003c\/li\u003e \u003cp\u003eSilvia Paoletta, Stephanie Federico, Giampiero Spalluto and Stefano Moro\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eInverse agonists of steroidogenic factor SF-1\u003c\/li\u003e \u003cp\u003eFabrice Piu and Andria L. Del Tredici\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMethods to Measure G Protein Coupled Receptor Activity for the Identification of Inverse Agonists\u003c\/li\u003e \u003cp\u003eGabriel Barreda-Gómez, M.Teresa Giralt and Rafael Rodríguez-Puertas\u003c\/p\u003e    \u003cp\u003eSection II-- Novel Strategies and Techniques for Constitutive Activity and Inverse Agonism\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eUse of Pharmacoperones to Reveal GPCR Structural Components Associated with Receptor Activation and Trafficking\u003c\/li\u003e \u003cp\u003eJo Ann Janovick and P. Michael Conn\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eApplication of large-scale transiently transfected cells to functional assays of ion channels and other proteins.\u003c\/li\u003e \u003cp\u003eJun Chen, Sujatha Gopalakrishnan, Marc R Lake, and Bruce R Bianchi\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eQuantification of RNA Editing of the Serotonin 2C Receptor (5-HT2CR) Ex Vivo \u003c\/li\u003e \u003cp\u003eMaria Fe Lanfranco, Noelle C. Anastasio, Patricia K. Seitz, and Kathryn A. Cunningham \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eStrategies for isolating constitutively-active and dominant-negative pheromone receptor mutants in yeast. \u003c\/li\u003e \u003cp\u003eMercedes Dosil and James B. Konopka\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eDevelopment of a GPR23 Cell-based ß-Lactamase Reporter Assay\u003c\/li\u003e \u003cp\u003ePaul H. Lee and Bonnie J. Hanson\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eComputational Modeling of Constitutively Active Mutants of GPCRs: C5a Receptor. \u003c\/li\u003e \u003cp\u003eGregory V. Nikiforovich and Thomas J. Baranski\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eTSH receptor monoclonal antibodies with agonist, antagonist and inverse agonist activities \u003c\/li\u003e \u003cp\u003eJane Sanders, Ricardo Núñez Miguel, Jadwiga Furmaniak, Bernard Rees Smith\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eCurrent standards, variations and pitfalls for the determination of constitutive TSHR activity in vitro\u003c\/li\u003e \u003cp\u003eSandra Mueller, Holger Jaeschke, Ralf Paschke \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eTowards the Rational Design of Constitutively Active KCa3.1 Mutant Channels \u003c\/li\u003e \u003cp\u003eLine Garneau, Hélène Klein, Lucie Parent, Rémy Sauvé\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eFusion proteins as model systems for the analysis of constitutive GPCR activity\u003c\/li\u003e \u003cp\u003eErich H. Schneider, Roland Seifert \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eScreening for Novel Constitutively Active CXCR2 Mutants and Their Cellular Effects \u003c\/li\u003e \u003cp\u003eGiljun Park, Tom Masi, Chang K. Choi, Heejung Kim, Jeffrey M. Becker, and Tim E. Sparer \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eA method for parallel solid-phase synthesis of iodinated analogues of the cannabinoid receptor type I (CB1) inverse agonist rimonabant \u003c\/li\u003e \u003cp\u003eAlan C. Spivey and Chih-Chung Tseng\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eCoexpression systems as models for the analysis of constitutive GPCR activity\u003c\/li\u003e \u003cp\u003eRoland Seifert and Erich H. Schneider\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eModelling and simulation of inverse agonism dynamics \u003c\/li\u003e \u003cp\u003eLloyd J. Bridge \u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eDesign and Use of Constitutively Active STAT5 Constructs \u003c\/li\u003e \u003cp\u003eMichael A. Farrar\u003c\/p\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eIn vitro and in vivo assays of protein kinase CK2 activity\u003c\/li\u003e \u003c\/ol\u003e \u003cp\u003eRenaud Prudent, Céline F. Sautel, Virginie Moucadel, Béatrice Laudet, Odilhe Filhol, and Claude Cochet\u003c\/p\u003e\n\u003c\/ol\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649313689880,"sku":"9780123812964","price":127.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123812964_e7049c9f-0b7f-481a-91bf-2f0b602fca2d.jpg?v=1695014008"},{"product_id":"serpin-structure-and-evolution-hardback-9780123859501","title":"Serpin Structure and Evolution (Hardback) 9780123859501","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eSerpin Structure and Evolution\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cp\u003eSerpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases, and this volume in the \u003ci\u003eMethods in Enzymology\u003c\/i\u003e series comprehensively covers this topic\u003c\/p\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eJames Whisstock (Volume editor), Phillip Bird (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123859501, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 5 December 2011\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e552 pages\u003cbr\u003e22.9 x 15.1 x 3.2 cm, 1.02 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eSerpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. This volume in the \u003ci\u003eMethods in Enzymology\u003c\/i\u003e series comprehensively covers this topic. With an international board of authors, this volume covers subjects such as Crystallography of serpins and serpin complexes, Serpins as hormone transporters, and Production of serpins using cell free systems.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e1. Development of inhibitors of PAI-1\u003c\/p\u003e \u003cp\u003eDaniel Lawrence \u003c\/p\u003e \u003cp\u003e2. Kinetics of Serpin interactions with cofactors and proteases\u003c\/p\u003e \u003cp\u003eSteven Olson \u003c\/p\u003e \u003cp\u003e3. Fluorescence Correlation Spectroscopy (FCS) or Single molecule FRET\u003c\/p\u003e \u003cp\u003eAnne Gershenson \u003c\/p\u003e \u003cp\u003e4. Serpin-enzyme receptors (LRP)\u003c\/p\u003e \u003cp\u003eDudley Strickland\u003c\/p\u003e \u003cp\u003e5. Predicting serpin \/ protease interactions\u003c\/p\u003e \u003cp\u003eJiangning Song \u003c\/p\u003e \u003cp\u003e6. Serpins and autophagy\u003c\/p\u003e \u003cp\u003eDavid Perlmutter \u003c\/p\u003e \u003cp\u003e7. Plant Serpins\u003c\/p\u003e \u003cp\u003eTom Roberts \u003c\/p\u003e \u003cp\u003e8. High throughput Drug discovery\u003c\/p\u003e \u003cp\u003eBibek Gooptu \u003c\/p\u003e \u003cp\u003e9. Use of mouse models to study maspin function\u003c\/p\u003e \u003cp\u003eMing Zhang \u003c\/p\u003e \u003cp\u003e10. The study of antitrypsin deficiency using animal models\u003c\/p\u003e \u003cp\u003eJeffrey Teckman \u003c\/p\u003e \u003cp\u003e11. Use of Mouse Models to study PAI-1\u003c\/p\u003e \u003cp\u003ePaul Declerck \u003c\/p\u003e \u003cp\u003e12. Production of serpins using cell free systems\u003c\/p\u003e \u003cp\u003eClifford Luke \u003c\/p\u003e \u003cp\u003e13. Studying serpin polymerisation in vitro\u003c\/p\u003e \u003cp\u003eJames Huntington \u003c\/p\u003e \u003cp\u003e14. Serpins and neural function \u003c\/p\u003e \u003cp\u003eDenis Monard \u003c\/p\u003e \u003cp\u003e15. Probing serpin conformational change using mass spectrometry and related methods\u003c\/p\u003e \u003cp\u003ePatrick Wintrode \u003c\/p\u003e \u003cp\u003e16. Studying Serpin conformational change\u003c\/p\u003e \u003cp\u003eRandy Read \u003c\/p\u003e \u003cp\u003e17. Production of serpins in bacteria\u003c\/p\u003e \u003cp\u003eMary Pearce \u003c\/p\u003e \u003cp\u003e18. Inhibition of cysteine proteases by serpins\u003c\/p\u003e \u003cp\u003eJan Potempa \u003c\/p\u003e \u003cp\u003e19. Post transcriptional regulation of serpins\u003c\/p\u003e \u003cp\u003eRob Medcalf \u003c\/p\u003e \u003cp\u003e20. Serpins and the complement system\u003c\/p\u003e \u003cp\u003eRob Pike \u0026amp; Lakshmi Wijeyewickrema \u003c\/p\u003e \u003cp\u003e21. Serpins in Caenorhabditis elegans\u003c\/p\u003e \u003cp\u003eStephen Pak \u0026amp; Gary Silverman \u003c\/p\u003e \u003cp\u003e22. PEDF and angiogenesis\u003c\/p\u003e \u003cp\u003ePatricia Becerra \u003c\/p\u003e \u003cp\u003e23. The Serpinb1 knockout mouse\u003c\/p\u003e \u003cp\u003eCharaf Benarafa \u003c\/p\u003e \u003cp\u003e24. Biophysical approaches to studying serpin folding\u003c\/p\u003e \u003cp\u003eSteve Bottomley \u003c\/p\u003e \u003cp\u003e25. TALS for studying the proteases inhibited by Serpins\u003c\/p\u003e \u003cp\u003eChris Overall \u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Enzymology [\u003ca title=\"See our other books on Enzymology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Enzymology%20%5BPSBZ%5D%22\"\u003ePSBZ\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biophysics [\u003ca title=\"See our other books on Biophysics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biophysics%20%5BPHVN%5D%22\"\u003ePHVN\u003c\/a\u003e], Therapy \u0026amp; therapeutics [\u003ca title=\"See our other books on Therapy \u0026amp; therapeutics\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Therapy%20\u0026amp;%20therapeutics%20%5BMMZ%5D%22\"\u003eMMZ\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649323356440,"sku":"9780123859501","price":132.59,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123859501.jpg?v=1695014096"},{"product_id":"activins-and-inhibins-hardback-9780123859617","title":"Activins and Inhibins (Hardback) 9780123859617","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eActivins and Inhibins\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003ci\u003eCutting-edge review concerning the molecular and cellular biology of vitamins and hormones\u003c\/i\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eGerald Litwack (Series edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123859617\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 20 April 2011\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e368 pages, 57 illustrations\u003cbr\u003e22.9 x 15.1 x 2.5 cm, 0.63 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eFirst published in 1943, \u003ci\u003eVitamins and Hormones\u003c\/i\u003e is the longest-running serial published by Academic Press. The Editorial Board now reflects expertise in the field of hormone action, vitamin action, X-ray crystal structure, physiology, and enzyme mechanisms. Under the capable and qualified editorial leadership of Dr. Gerald Litwack, \u003ci\u003eVitamins and Hormones\u003c\/i\u003e continues to publish cutting-edge reviews of interest to endocrinologists, biochemists, nutritionists, pharmacologists, cell biologists, and molecular biologists. Others interested in the structure and function of biologically active molecules like hormones and vitamins will, as always, turn to this series for comprehensive reviews by leading contributors to this and related disciplines.This volume focuses on activins and inhibins.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Animal physiology [\u003ca title=\"See our other books on Animal physiology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Animal%20physiology%20%5BPSVD%5D%22\"\u003ePSVD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Endocrinology [\u003ca title=\"See our other books on Endocrinology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Endocrinology%20%5BMJG%5D%22\"\u003eMJG\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46649324994840,"sku":"9780123859617","price":137.49,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123859617_d337f59c-b716-4243-8bcc-37e8abb1d69c.jpg?v=1694352163"},{"product_id":"computational-chemistry-methods-in-structural-biology-hardback-9780123864857","title":"Computational Chemistry Methods in Structural Biology (Hardback) 9780123864857","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eComputational Chemistry Methods in Structural Biology\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cp\u003ePublished continuously since 1944, the\u003ci\u003e Advances in Protein Chemistry and Structural Biology\u003c\/i\u003e serial has been a continuous, essential resource for protein chemists, and this volume features articles on Computational Chemistry methods in Structural Biology\u003c\/p\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eChristo Christov (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123864857\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 3 November 2011\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e360 pages\u003cbr\u003e22.9 x 15.1 x 2.5 cm, 0.71 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003ePublished continuously since 1944, the\u003ci\u003e Advances in Protein Chemistry and Structural Biology\u003c\/i\u003e serial has been a continuous, essential resource for protein chemists. Covering reviews of methodology and research in all aspects of protein chemistry, including purification\/expression, proteomics, modeling and structural determination and design, each volume brings forth new information about protocols and analysis of proteins while presenting the most recent findings from leading experts in a broad range of protein-related topics. This volume features articles on Computational Chemistry methods in Structural Biology.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003col\u003e \u003cli\u003eNew computational strategies for designing enzyme inhibitors Juan Andres\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eTheoretical Investigation of enzyme-inhibitor interactions Alessio Lodola\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRecent advances in molecular modelling of endocrine disruptors Ivanka Tsakovska\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMultiscale Simulation Methods for Mapping Conformational Ensembles of G-Protein Coupled Receptors Nagarajan Vaidehi\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdvances in implicit models of water solvent for method vof molecular dynamics and applications to study macromolecular complexes, ligand docking and pH-dependent effects Yury Vorobjev\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eFree Energy Methods for the Prediction and Analysis of Protein-Ligand Binding Affinities Emilio Gallicchio\u003c\/li\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eCoarse-Grained Modelling of Protein Flexibility Modesto Orozco\u003c\/li\u003e\n\u003c\/ol\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46649325551896,"sku":"9780123864857","price":115.49,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123864857_ddc5530f-584b-489a-ba56-4df40bfa9f92.jpg?v=1694352158"},{"product_id":"the-molecular-biology-of-cadherins-hardback-9780123943118","title":"The Molecular Biology of Cadherins (Hardback) 9780123943118","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eThe Molecular Biology of Cadherins\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eWritten by research experts in that specialize in the field, this volume of \u003ci\u003eProgress in Molecular Biology and Translational Science\u003c\/i\u003e focuses on the most recent research surrounding cadherins and provides insight into future applications\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eFrans Van Roy (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123943118, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 10 May 2013\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e488 pages\u003cbr\u003e22.9 x 15.1 x 2.9 cm, 0.77 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\u003cp\u003ePraise for the series: \"Full of interest not only for the molecular biologist-for whom the numerous references will be invaluable-but will also appeal to a much wider circle of biologists, and in fact to all those who are concerned with the living cell.\"\u003cb\u003e --British Medical Journal\u003c\/b\u003e\u003c\/p\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThis volume of \u003ci\u003eProgress in Molecular Biology and Translational Science\u003c\/i\u003e focuses on the most recent research surrounding Cadherins from top experts in the field.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eStability and dynamics of cell-cell junctions\u003c\/p\u003e \u003cp\u003eT. Lecuit\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eSignaling by classical cadherin adhesion receptors\u003c\/p\u003e \u003col\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eYap\u003c\/li\u003e \u003c\/ol\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eNew insights into the evolution of metazoan cadherins\u003c\/p\u003e \u003cp\u003eP. Hulpiau\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eWhere the cadherins root: the diverse junctional plaques\u003c\/p\u003e \u003cp\u003eS. Rickelt\u003c\/p\u003e\n\u003cb\u003e\u003ci\u003e \u003c\/i\u003e\u003c\/b\u003e\u003cp\u003eStructure, function and regulation of desmosomes\u003c\/p\u003e \u003col\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eKowalczyk\u003c\/li\u003e \u003c\/ol\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eVE-cadherin and vascular morphogenesis\u003c\/p\u003e \u003cp\u003eE. Dejana\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eNeuronal diversity by clustered protocadherins\u003c\/p\u003e \u003cp\u003eT. Yagi\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eDelta-protocadherins in health and disease\u003c\/p\u003e \u003col\u003e \u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eKahr\u003c\/li\u003e \u003c\/ol\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eRole of Celsr-1 to -3 in mouse brain development\u003c\/p\u003e \u003cp\u003eC Boutin\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eN-cadherin function in development and disease\u003c\/p\u003e \u003cp\u003eG. Radice\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eCadherin dynamics during neural crest cell ontogeny\u003c\/p\u003e \u003cp\u003eL. Taneyhill\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eCadherins and EMT: Regulation in normal tissue homeostasis and related pathologies\u003c\/p\u003e \u003cp\u003eG. Berx\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eCadherin abnormalities in familial cancers\u003c\/p\u003e \u003cp\u003eF. Caneiro\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eThe other catenins: challenging our current view of canonical Wnt signaling\u003c\/p\u003e \u003cp\u003eP. Mccrea\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003eAfadin\/AF6\/Canoe: Roles in the organization of junctional complexes\u003c\/p\u003e \u003cp\u003eK. Mandai\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Cellular biology [\u003ca title=\"See our other books on Cellular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Cellular%20biology%20%5Bcytology%5D%20%5BPSF%5D%22\"\u003ecytology PSF\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Metabolism [\u003ca title=\"See our other books on Metabolism\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Metabolism%20%5BMFGM%5D%22\"\u003eMFGM\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649330762008,"sku":"9780123943118","price":103.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123943118.jpg?v=1694099769"},{"product_id":"bio-nanoimaging-protein-misfolding-and-aggregation-hardback-9780123944313","title":"Bio-nanoimaging; Protein Misfolding and Aggregation (Hardback) 9780123944313","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eBio-nanoimaging\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eProtein Misfolding and Aggregation\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cem\u003eThis content provides researchers and clinicians alike with information important to drug design studies and the development of novel treatments for protein misfolding diseases\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eVladimir N Uversky (Edited by), Yuri Lyubchenko (Edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123944313\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 7 January 2014\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e552 pages, 300 illustrations (200 in full color)\u003cbr\u003e27.6 x 21.5 x 3.2 cm, 1.71 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\"Among the topics are conformation-dependent antibodies as tools for characterizing amyloid protein aggregates, studying the molecular determinants of protein oligomerization in neurodegenerative disorders by bimolecular fluorence complimentation, possible function and toxicity of multiple oligomeric\/conformational states of the globular protein human stefin B…\" \u003cb\u003e--ProtoView.com, February 2014\u003c\/b\u003e \u003c\/p\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\u003ci\u003eBio-Nanoimaging: Protein Misfolding \u0026amp; Aggregation\u003c\/i\u003e provides a unique introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. The book is divided into three sections covering:- Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits - Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and insulin oligomers- Polymorphisms of misfolding and aggregation processes, including multiple pathways of lysozyme aggregation, misfolded intermediate of a PDZ domain, and micelle formation by human islet amyloid polypeptide\u003c\/p\u003e  \u003cp\u003eProtein misfolding and aggregation is a fast-growing frontier in molecular medicine and protein chemistry. Related disorders include cataracts, arthritis, cystic fibrosis, late-onset diabetes mellitus, and numerous neurodegenerative diseases like Alzheimer's and Parkinson's. Nanoimaging technology has proved crucial in understanding protein-misfolding pathologies and in potential drug design aimed at the inhibition or reversal of protein aggregation. Using these technologies, researchers can monitor the aggregation process, visualize protein aggregates and analyze their properties.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\u003cb\u003ePart 1. Nanotechnology and nanoimaging of aggregating proteins\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eNanoimaging of aggregated proteins; Cryoelectron microscopy of beta(2)-microglobulin; Amyloid fibril length quantification by AFM; Seeing fibril formation in real time; Studying amyloidogensis by FRET;   Structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy; Analyzing amyloid fibril structure by scanning transmission electron microscopy; Magic angle spinning NMR of amyloid fibrils; Analyzing protein deposits in vivo by confocal laser multiphoton laser scanning microscopy; Amyloid imaging agents; Reporters of amyloid structure; Immunohistochemical detection of amyloid components; Scanning tunneling microscopy of protein deposits; Probing of protein misfolding with single molecule force spectroscopy; Single molecule characterization of a-synuclein in aggregation-prone states\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 2. Polymorphism of protein misfolded and aggregated species\u003c\/b\u003e \u003c\/p\u003e \u003cp\u003eFibrillar polymorphism; Ab fibril polymorphism; Prefibrillar Ab oligomers; Structural heterogeneity of in vitro and ex vivo  amyloid assemblies; Polymorphism of tau fibrils; Amyloid-like protofibrils with different physical properties; Micelle-Like Architecture of the Amyloid-ß Peptide; Insulin oligomers; Worm-like amyloid fibrils of mouse prion protein; Apolipoprotein C-II Amyloid Fibrils; Amylin oligomers and fibrils;  Amyloid fibrils of human stefins; Fibrillar structure of Sup35 in vivo; Dopamine-induced a-synuclein oligomers ; Amyloid spherulites; A stable lipid-induced aggregate of alpha-synuclein \u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 3. Polymorphism of protein misfolding and aggregation processes\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eMultiple pathways of lysozyme aggregation; Structure-function study of amyloid ion channels in neurodegenerative diseases; Amyloid ß-protein assembly; Molecular mechanisms underlying alpha synucelin misassembly; Multiple pathways of amyloid assembly \/disassembly studied by AFM; Sequestering of metastable proteins with essential cellular functions by amyloid-like aggregates; Misfolded intermediate of a PDZ domain; Structural characterization of the amyloidogenic state of human lysozyme; Landscape Model of Filamentous Protein Aggregation; Micelle formation by human islet amyloid polypeptide; Effect of anionic polysaccharide on ß-lactoglobulin fibrillation\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Biomedical engineering [\u003ca title=\"See our other books on Biomedical engineering\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biomedical%20engineering%20%5BMQW%5D%22\"\u003eMQW\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46649331384600,"sku":"9780123944313","price":93.59,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123944313_43b30c6a-def0-4076-96d3-a54d2a7e3a31.jpg?v=1694352189"},{"product_id":"the-molecular-biology-of-arrestins-hardback-9780123944405","title":"The Molecular Biology of Arrestins (Hardback) 9780123944405","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eThe Molecular Biology of Arrestins\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThis special volume of \u003ci\u003eProgress in Molecular Biology and Translational Science \u003c\/i\u003efocuses on the molecular biology of arrestins, with contributions from leaders in the field\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eLouis M. Luttrell (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123944405, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 31 July 2013\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e536 pages\u003cbr\u003e22.9 x 15.1 x 3.1 cm, 0.78 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\u003cp\u003ePraise for the series: \"Full of interest not only for the molecular biologist-for whom the numerous references will be invaluable-but will also appeal to a much wider circle of biologists, and in fact to all those who are concerned with the living cell.\"\u003cb\u003e --British Medical Journal\u003c\/b\u003e\u003c\/p\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eThis special volume of \u003ci\u003eProgress in Molecular Biology and Translational Science \u003c\/i\u003efocuses on the molecular biology of arrestins, with contributions from leaders in the field. Arrestins have emerged as central players in the regulation of many facets of G protein-coupled receptor signaling. This volume covers a variety of topics with reviews written by experts in the field.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\u003cb\u003ePart I: Perspective - The Duality of Arrestin Function\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1. \u003c\/b\u003e\u003cb\u003eArrestins Come of Age: A Personal Historical Perspective\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart II: The Molecular Biology of Arrestins\u003c\/b\u003e\u003c\/p\u003e \u003col\u003e \u003c\/ol\u003e \u003cp\u003e2. True Arrestins and Arrestin-Fold Proteins: A Structure-Based Appraisal\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e3. Structural Determinants of Arrestin Functions\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e4. Arrestins: Role in the Desensitization, Sequestration and Vesicular Trafficking of G Protein-Coupled Receptors\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e5. Arrestins as Regulators of Kinases and Phosphatases\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e6. ß-Arrestins: Modulators of Small GTPase Activation and Function\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e7. Arrestins and Protein Ubiquitination\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e8. Arrestins in Actin Reorganization and Cell Migration\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart III: The Physiological Roles of Arrestins\u003c\/b\u003e\u003c\/p\u003e \u003col\u003e \u003c\/ol\u003e \u003cp\u003e9. The Role of Arrestins in Development\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e10. The Role of Arrestins in Visual and Disease Processes of the Eye\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e11. b-Arrestins in the Central Nervous System\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e12. Arrestins in the Cardiovascular System\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e13. Arrestins in Bone\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e14. b-Arrestins in the Immune System\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e15. The Role of b-Arrestins in Cancer\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e16. Arrestins in Metabolic Regulation\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart IV: The Future - The Potential for Arrestin-based Therapeutics\u003c\/b\u003e\u003c\/p\u003e \u003col\u003e \u003c\/ol\u003e \u003cp\u003e17. Systems Analysis of Arrestin Pathway Functions\u003c\/p\u003e \u003col\u003e \u003cb\u003e \u003c\/b\u003e\n\u003c\/ol\u003e \u003cp\u003e18. Arrestin Pathways as Drug Targets\u003c\/p\u003e \u003col\u003e \u003c\/ol\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Clinical \u0026amp; internal medicine [\u003ca title=\"See our other books on Clinical \u0026amp; internal medicine\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Clinical%20\u0026amp;%20internal%20medicine%20%5BMJ%5D%22\"\u003eMJ\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649332564248,"sku":"9780123944405","price":105.79,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123944405.jpg?v=1694099781"},{"product_id":"methods-in-protein-design-hardback-9780123942920","title":"Methods in Protein Design (Hardback) 9780123942920","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eMethods in Protein Design\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cp\u003eThis new volume of \u003ci\u003eMethods in Enzymology\u003c\/i\u003e continues the legacy of this premier serial with quality chapters authored by leaders in the field. This volume covers methods in protein design, including such topics as protein switch engineering by domain insertion, evolution-based design of proteins, and computationally designed proteins.\u003c\/p\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eAmy Keating (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123942920\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 17 April 2013\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e520 pages\u003cbr\u003e22.9 x 15.1 x 3.1 cm, 0.82 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eApprox.466 pages\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003col\u003e\n\u003cb\u003e \u003cli\u003eComputational Design of Novel Protein Binders and Experimental Affinity Maturation\u003cbr\u003e\n\u003c\/li\u003e\u003c\/b\u003e\u003cb\u003e \u003cli\u003eMining Tertiary Structural Motifs for Assessment of Designability\u003cbr\u003e\n\u003c\/li\u003e \u003cli\u003e\u003c\/b\u003e\u003cb\u003eComputational Methods for Controlling Binding Specificity \u003c\/b\u003e\u003cb\u003e \u003cli\u003eFlexible Backbone Sampling Methods to Model and Design Protein Alternative Conformations\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eOSPREY: Protein Design with Ensembles, Flexibility, and Provable Algorithms\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eScientific Benchmarks for Guiding Macromolecular Energy Function Improvement\u003cbr\u003e\n\u003c\/li\u003e \u003cli\u003e\u003c\/b\u003e\u003cb\u003eMolecular Dynamics Simulations for the Ranking, Evaluation, and Refinement of Computationally Designed Proteins \u003c\/b\u003e\u003cb\u003e \u003cli\u003eMulti-State Protein Design Using CLEVER and CLASSY\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eUsing Analyses of Amino Acid Coevolution to Understand Protein Structure and Function\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eEvolution Based Design of Proteins\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eProtein Engineering and Stabilization from Sequence Statistics: Variation and Co-Variation Analysis\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eEnzyme Engineering by Targeted Libraries\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eGeneration of High-Performance Binding Proteins for Peptide Motifs by Affinity Clamping\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eEngineering Fibronectin-Based Binding Proteins by Yeast Surface Display\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eEngineering and Analysis of Peptide-Recognition Domain Specificities by Phage Display and Deep Sequencing\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eEfficient Sampling of SCHEMA Chimera Families to Identify Useful Sequence Elements\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eProtein Switch Engineering by Domain Insertion\u003c\/li\u003e \u003c\/b\u003e\u003cb\u003e \u003cli\u003eDesign of Chimeric Proteins by Combination of Subdomain-Sized Fragments\u003cbr\u003e\n\u003c\/li\u003e \u003cli\u003e\u003c\/b\u003e\u003cb\u003ea-Helix Mimicry with a\/ß-Peptides \u003c\/b\u003e\n\u003c\/ol\u003e\n\u003ci\u003e \u003c\/i\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Biotechnology [\u003ca title=\"See our other books on Biotechnology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biotechnology%20%5BTCB%5D%22\"\u003eTCB\u003c\/a\u003e], Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46649333252376,"sku":"9780123942920","price":120.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123942920.jpg?v=1694099788"},{"product_id":"adiponectin-hardback-9780123983138","title":"Adiponectin (Hardback) 9780123983138","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eAdiponectin\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003e\u003cp\u003eCutting-edge review concerning the molecular and cellular biology of vitamins and hormones\u003c\/p\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eGerald Litwack (Series edited by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123983138\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 13 November 2012\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e480 pages\u003cbr\u003e22.9 x 15.1 x 2.9 cm, 0.75 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eApprox.460 pages\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003col\u003e\n\u003cb\u003e \u003cli\u003eLifestyle Factors Increasing Adiponectin Synthesis and Secretion\u003c\/li\u003e\u003c\/b\u003e\u003ci\u003e \u003c\/i\u003e\u003cp\u003eJustine M. Tishinsky, David J. Dyck, Lindsay E. Robinson\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eMolecular Tools to Characterize Adiponectin Activity\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eCathleen Juhl and Annette G. Beck-Sickinger\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eNutritional and Hormonal Modulation of Adiponectin and Its Receptors AdipoR1 and AdipoR2\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eCristiane de Oliveira, Ana Barbosa Marcondes de Mattos, Carolina Biz Rodrigues Silva, João Felipe Mota, Juliane Costa Silva Zemdegs\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eRegulation and Function of Adiponectin Receptors in Skeletal Muscle \u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eYaniv Lustig, Rina Hemi and Hannah Kanety\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eScreening for Adiponectin Secretion Regulators\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eKyosuke Hino and Hidetaka Nagata\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdiponectin and PPAR?: Cooperative and Interdependent Actions of Two Key Regulators of Metabolism \u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eOlga Astapova and Todd Leff\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eGlucocorticoid Effects on Adiponectin Expression\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eSiddharth Sukumaran, Debra C. DuBois, William J. Jusko, and Richard R. Almon\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdiponectin and Reproduction\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eEsther Dos Santos, René Pecquery, Philippe De Mazancourt and Marie-Noëlle Dieudonne\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdiponectin and Its Receptors in Preimplantation Embryo Development \u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eŠtefan Cikoš\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdiponectin and the Control of Female Reproductive Functions\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eMarie-France Palin, Vilceu Bordignon V and Bruce D. Murphy\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdiponectin in the Heart and Vascular System\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eMin Ding, Eva M. Rzucidlo, Jennifer C. Davey, Yi Xie, Renjing Liu, Yu Jin, Lindsey Stavola, and Kathleen A. Martin\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdiponectin Interactions In Bone and Cartilage Biology And Disease\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eMassimiliano Ruscica, Liliana Steffani, and Paolo Magni\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eLipid-Lowering Drugs and Circulating Adiponectin\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eDesiree Wanders, Eric P. Plaisance, Robert L. Judd\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdiponectin And Interleukin-6 In Inflammation-Associated Disease\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eLi Li, and Li-Ling Wu\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eNew Insights into Anti-Carcinogenic Properties of Adiponectin: a Potential Therapeutic Approach in Breast Cancer?\u003c\/li\u003e \u003ci\u003e \u003c\/i\u003e\u003cp\u003eLaetitia Delort, Thierry Jardé, Virginie Dubois, Marie-Paule Vasson, Florence Caldefie-Chézet\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003cp\u003e \u003c\/p\u003e\n\u003cli\u003eAdiponectin: A Novel Link between Adipocytes and COPD \u003c\/li\u003e \u003c\/ol\u003e\n\u003ci\u003e \u003c\/i\u003e\u003cp\u003eYoshito Takeda, Kaori Nakanishi, Isao Tachibana, Atsushi Kumanogoh\u003c\/p\u003e\n\u003cb\u003e \u003c\/b\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Molecular biology [\u003ca title=\"See our other books on Molecular biology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Molecular%20biology%20%5BPSD%5D%22\"\u003ePSD\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46649338233112,"sku":"9780123983138","price":144.99,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123983138.jpg?v=1694099822"},{"product_id":"protein-kinase-inhibitors-in-research-and-medicine-hardback-9780123979186","title":"Protein Kinase Inhibitors in Research and Medicine (Hardback) 9780123979186","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eProtein Kinase Inhibitors in Research and Medicine\u003c\/font\u003e\u003cbr\u003e\r\n\r\n\r\n\u003c\/p\u003e\n\u003cp\u003e\u003cem\u003eThis new volume of \u003ci\u003eMethods in Enzymology\u003c\/i\u003e continues the legacy of this premier serial with quality chapters authored by leaders in the field.\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eKevan M Shokat (Volume editor)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780123979186, Elsevier Science\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 12 November 2014\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e252 pages\u003cbr\u003e22.9 x 15.1 x 2.1 cm, 0.61 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003eThis new volume of \u003ci\u003eMethods in Enzymology\u003c\/i\u003e continues the legacy of this premier serial with quality chapters authored by leaders in the field. This volume covers protein kinase inhibitors in research and medicine, and includes chapters on such topics as fragment-based screening, broad kinome profiling of kinase inhibitors, and designing drug-resistant kinase alleles.\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e1. Catalytic Mechanisms and Regulation of Protein Kinases\u003cbr\u003eZhihong Wang and Philip A. Cole.\u003cbr\u003e2. A Structural Atlas of Kinases Inhibited by Clinically Approved Drugs\u003cbr\u003eQi Wang, Julie A. Zorn and John Kuriyan.\u003cbr\u003e3. Fragment-Based Approaches to the Discovery of Kinase Inhibitors\u003cbr\u003ePaul N. Mortenson, Valerio Berdini and Marc O’Reilly.\u003cbr\u003e4. Targeting Protein Kinases with Selective and Semi-Promiscuous Covalent Inhibitors\u003cbr\u003eRand M. Miller and Jack Taunton.\u003cbr\u003e5. The Resistance Tetrad: Amino Acid Hotspots for Kinome-Wide Exploitation of Drug-resistant Protein Kinase Alleles\u003cbr\u003eVeselin I Andreev and Patrick A Eyers\u003cbr\u003e6. FLiK: A Direct Binding Assay for the Identification and Kinetic Characterization of Stabilizers of Inactive Kinase Conformations \u003cbr\u003eJeffrey R. Simar and Daniel Rauh\u003cbr\u003e7. Discovery of Allosteric Bcr-Abl inhibitors from Phenotypic Screen to Clinical Candidate\u003cbr\u003eNathanael S. Gray and Doriano Fabbro\u003cbr\u003e8. The Logic and Design of Analog-Sensitive (AS) Kinases and their Small Molecule Inhibitors\u003cbr\u003eMichael S. Lopez, Joseph Kliegman and Kevan M. Shokat\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Enzymology [\u003ca title=\"See our other books on Enzymology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Enzymology%20%5BPSBZ%5D%22\"\u003ePSBZ\u003c\/a\u003e], Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], Pharmacology [\u003ca title=\"See our other books on Pharmacology\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Pharmacology%20%5BMMG%5D%22\"\u003eMMG\u003c\/a\u003e], Clinical \u0026amp; internal medicine [\u003ca title=\"See our other books on Clinical \u0026amp; internal medicine\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Clinical%20\u0026amp;%20internal%20medicine%20%5BMJ%5D%22\"\u003eMJ\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Academic Press","offers":[{"title":"Default Title","offer_id":46649339248920,"sku":"9780123979186","price":93.59,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780123979186.jpg?v=1694099830"},{"product_id":"low-abundance-proteome-discovery-state-of-the-art-and-protocols-paperback-9780124017344","title":"Low-Abundance Proteome Discovery; State of the Art and Protocols (Paperback \/ softback) 9780124017344","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eLow-Abundance Proteome Discovery\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eState of the Art and Protocols\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cem\u003e\u003cp\u003eThis book addresses the biggest challenge in the field of protein biomarkers – detecting low-abundance proteomes – and offers novel methods and protocols for their detection, identification, and quantification.\u003c\/p\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eEgisto Boschetti (Author), Pier Giorgio Righetti (Author)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9780124017344\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003ePaperback \/ softback, published 16 May 2013\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e364 pages, Illustrated\u003cbr\u003e27.6 x 21.5 x 2.3 cm, 1.11 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cem\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\"The book was written by the inventors of and leading experts in the technology and provides a comprehensive overview of what has been achieved with this relatively new approach. The detailed description of important experimental parameters and the protocols provided in this book make it a unique resource for all practitioners in the field and all scientists interested in the technology.\" --\u003cb\u003eAnalytical \u0026amp; Bioanalytical Chemistry, February 2014\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\"Boschetti and Righetti introduce the new technique of combinatorial peptide ligand libraries for identifying low-abundance peptide fragments. The standard proteomics techniques of mass spectrometry, 2D electrophoresis and chromatography are deliberately given brief treatment only as prefractionation tools in favor of new methodologies.\" --\u003cb\u003eReference \u0026amp; Research Book News, October 2013\u003c\/b\u003e\u003c\/p\u003e\u003c\/font\u003e\u003c\/em\u003e\u003c\/p\u003e\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\u003ci\u003eLow-Abundance Proteome Discovery\u003c\/i\u003e addresses the most critical challenge in biomarker discovery and progress: the identification of low-abundance proteins. The book describes an original strategy developed by the authors that permits the detection of protein species typically found in very low abundance and that may yield valuable clues to future discoveries. Known as combinatorial peptide ligand libraries, these new methodologies are one of the hottest topics related to the study of proteomics and have applications in medical diagnostics, food quality, and plant analysis. The book is written for university and industry scientists starting proteomic studies of complex matrices (e.g., biological fluids, biopsies, recalcitrant plant tissues, foodstuff, and beverage analysis), researchers doing wet chemistry, and graduate-level students in the areas of analytical and biochemistry, biology, and genetics.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eAntiphon1. Introducing low-abundance species in proteome analysis2. Chromatographic and electrophoretic pre-fractionation tools in proteome analysis3. Current low-abundance protein access4. Low-abundance protein access by combinatorial peptide libraries5. Plant proteomics and food and beverage analysis via CPLL capture6. Biomedical involvements of low-abundance proteins7. Other applications of combinatorial peptide libraries8. Detailed methodologies and protocolsPolyphony\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Proteins [\u003ca title=\"See our other books on Proteins\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Proteins%20%5BPSBC%5D%22\"\u003ePSBC\u003c\/a\u003e], Biochemistry [\u003ca title=\"See our other books on Biochemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Biochemistry%20%5BPSB%5D%22\"\u003ePSB\u003c\/a\u003e], DNA \u0026amp; Genome [\u003ca title=\"See our other books on DNA \u0026amp; Genome\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22DNA%20\u0026amp;%20Genome%20%5BPSAK1%5D%22\"\u003ePSAK1\u003c\/a\u003e], Analytical chemistry [\u003ca title=\"See our other books on Analytical chemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Analytical%20chemistry%20%5BPNF%5D%22\"\u003ePNF\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Freshly Printed Books","offers":[{"title":"Default Title","offer_id":46649340821784,"sku":"9780124017344","price":67.19,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/products\/9780124017344_ef1a7a43-3c17-4a6f-afb2-857a1e2fa6ec.jpg?v=1694352968"}],"url":"https:\/\/freshlyprintedbooks.co.uk\/collections\/proteins.oembed?page=3","provider":"Freshly Printed Books","version":"1.0","type":"link"}