Structure and Intrinsic Disorder in Enzymology

Herausgeber: Gupta, Munishwar Nath; Uversky, Vladimir N

• Broschiertes Buch

Produktbeschreibung

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.

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Produktdetails

• Verlag: Elsevier Science
• Seitenzahl: 528
• Erscheinungstermin: 21. November 2022
• Englisch
• Gewicht: 1040g
• ISBN-13: 9780323995337
• ISBN-10: 0323995330
• Artikelnr.: 63563730

Inhaltsangabe

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