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.
- Unifies the roles of intrinsic disorder and structure in the functioning of enzymes and proteins
- Examines a range of enzyme and protein characteristics, their relationship to intrinsic disorder, and methods for study
- Features chapter contributions from international leaders in the field
Sprache
Verlagsort
Verlagsgruppe
Elsevier Science & Techn.
Dateigröße
ISBN-13
978-0-323-99534-4 (9780323995344)
Schweitzer Klassifikation
1. Enzymology: Early insights2. Deep mutational scanning to probe specificity determinants.3. Protein flexibility and cryo-enzymology: The trade-off between stability andcatalytic rates4. Thermodynamic Perspective of Protein Disorder and Phase Separation: Model Systems5. Structure and disorder: Protein functions depend on this new binary transforming lock-and-key into structure-function continuum6. Methods for measuring structural disorder in proteins7. Prediction of protein structure and intrinsic disorder in the era of deep learning8. Roles of Intrinsically Disordered Regions in Phosphoinositide 3-Kinase Biocatalysis9. Many faces of protein promiscuity: Not just broad specificity of proteins10. Role Of Plasticity And Disorder In Protein Moonlighting: Blurring Of Lines Between Biocatalysts And Other Biologically Active Proteins11. Molten globular enzymes12. Intrinsic disorder and allosteric regulation13. Macromolecular Crowding: How it Affects Protein Structure, Disorder, and Catalysis14. Intrinsic disorder and post-translational modifications: An evolutionary perspective15. The roles of prion-like domains in amyloid formation, phase separation, and solubility16. IDPRs of membrane proteins influence membrane curvature17. How binding to surfaces affects disorder
