Structure and Intrinsic Disorder in Enzymology
Series: Foundations and Frontiers in Enzymology;
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Product details:
- Publisher Elsevier Science
- Date of Publication 21 November 2022
- ISBN 9780323995337
- Binding Paperback
- No. of pages528 pages
- Size 234x190 mm
- Weight 1040 g
- Language English 414
Categories
Long description:
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.
Chapters also review methods for study, as well as evolving technology to support new research across academic, industrial and pharmaceutical labs.
MoreTable of Contents:
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
