Freshly Printed - allow 10 days lead
Couldn't load pickup availability
Protein NMR Spectroscopy
Principles and Practice
Key resource for NMR Spectroscopy!
John Cavanagh (Author), Nicholas J. Skelton (Author), Wayne J. Fairbrother (Author), Mark Rance (Author), Arthur G. Palmer III (Author)
9780121644918, Elsevier Science
Hardback, published 13 December 2006
912 pages, Approx. 250 illustrations
22.9 x 15.1 x 4.4 cm, 1.33 kg
"This volume is a comprehensive introduction to the methodology required for NMR studies of proteins." --JOURNAL OF MAGNETIC RESONANCE "Protein NMR Spectroscopy: Principles and Practice covers a huge range of topics related to NMR....A fine two-semester course could be built on this very thorough book. Any student currently using NMR could benefit from the Cavanagh et al. text, which provides an in-depth explanation that is suitable as a resource for even a knowledgeable spectroscopist." --NATURE STRUCTURAL BIOLOGY "All in all, I find the book very, very good. It will fill an important void in the literature/material available in the NMR field.....There are many 'hands on' secrets that will be very valuable to those beginning in the field as well as those who are 'old hands.' It has a distinct advantage over other books in that is was written as a whole, freshly from cover to cover; it is NOT a collection of published articles hurriedly put together with a nice binding." --DALE F. MIERKE, UNIVERSITY OF MASSACHUSETTS, AMHERST "Along with detailed explanations of the mechanisms underlying the modern NMR experiments, the book also brings some "order" to the bewildering array of novel NMR pulse sequences. To practitioners of biomolecular NMR, it will prove invaluable for years to come." --STRUCTURE
Protein NMR Spectroscopy, Second Edition combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, the book develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments. Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. This updated version includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced. The book is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or wish to understand the latest developments in this field.
1: Classical NMR Spectroscopy 2: Theoretical Description of NMR Spectroscopy 3: Experimental Aspects of NMR Spectroscopy 4: Multidimensional NMR Spectroscopy 5: Relaxation and Dynamic Processes 6: Experimental 1h NMR Methods 7: Heteronuclear NMR Experiments 8: Experimental NMR Relaxation Methods 9: Larger Proteins and Molecular Interactions 10: Sequential Assignment, Structure Determination, and other Applications
Subject Areas: Cellular biology [cytology PSF], Biochemistry [PSB], Spectrum analysis, spectrochemistry, mass spectrometry [PNFS], Electricity, electromagnetism & magnetism [PHK]
