Structure and Intrinsic Disorder in Enzymology

Provides a thorough, practical overview of fundamental concepts, characteristics and functions of intrinsically disordered enzymes

Munishwar Nath Gupta (Edited by), Vladimir N. Uversky (Edited by)

9780323995337, Elsevier Science

Paperback, published 21 November 2022

528 pages, 60 illustrations (30 in full color)
23.4 x 19 x 3.3 cm, 1.04 kg

Structure and Intrinsic Disorder in Enzymology offers a direct, yet comprehensive presentation of the fundamental concepts, characteristics and functions of intrinsically disordered enzymes, along with valuable notes and technical insights powering new research in this emerging field. Here, more than twenty international experts examine protein flexibility and cryo-enzymology, hierarchies of intrinsic disorder, methods for measurement of disorder in proteins, bioinformatics tools for predictions of structure, disorder and function, protein promiscuity, protein moonlighting, globular enzymes, intrinsic disorder and allosteric regulation, protein crowding, intrinsic disorder in post-translational, and much more.

1. Enzymology: Early insights 2. Deep mutational scanning to probe specificity determinants. 3. Protein flexibility and cryo-enzymology: The trade-off between stability andcatalytic rates 4. Thermodynamic Perspective of Protein Disorder and Phase Separation: Model Systems 5. Structure and disorder: Protein functions depend on this new binary transforming lock-and-key into structure-function continuum 6. Methods for measuring structural disorder in proteins 7. Prediction of protein structure and intrinsic disorder in the era of deep learning 8. Roles of Intrinsically Disordered Regions in Phosphoinositide 3-Kinase Biocatalysis 9. Many faces of protein promiscuity: Not just broad specificity of proteins 10. Role Of Plasticity And Disorder In Protein Moonlighting: Blurring Of Lines Between Biocatalysts And Other Biologically Active Proteins 11. Molten globular enzymes 12. Intrinsic disorder and allosteric regulation 13. Macromolecular Crowding: How it Affects Protein Structure, Disorder, and Catalysis 14. Intrinsic disorder and post-translational modifications: An evolutionary perspective 15. The roles of prion-like domains in amyloid formation, phase separation, and solubility 16. IDPRs of membrane proteins influence membrane curvature 17. How binding to surfaces affects disorder

Subject Areas: Molecular biology [PSD], Enzymology [PSBZ], Biochemistry [PSB], Biophysics [PHVN]