Intrinsically Disordered Proteins: Dynamics, Binding, and Function thoroughly examines and ties together the fundamental biochemical functions of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs), including signaling, binding, and regulation, with the methodology for study and the associated pathways for drug design and therapeutic intervention. The role of new mechanistic, computational, and experimental approaches in IDP study are explored in depth, with methods for the characterization of IDP dynamics; models, simulations, and mechanisms of IDP and IDR binding; and biological and medical implications of IDP dynamics prominently featured. Written and edited by leading scientists in the field, this book explores groundbreaking areas such as ensemble descriptions of IDPs and IDRs, single-molecule studies of IDPs and IDRs, IDPs and IDRs in membraneless organelles, and molecular mechanisms of fibrillation of IDPs.
Intrinsically Disordered Proteins provides students and researchers in biochemistry, molecular biology, and applied microbiology with a comprehensive and updated discussion of the complex dynamics of IDPs and IDRs.
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Table of Contents
1. Introduction to intrinsically disordered proteins and regions
PART I Methodology 2. Ensemble descriptions of IDPs and IDRs: Integrating simulation and experiment 3. Experimental characterization of the dynamics of IDPs and IDRs by NMR 4. Single-molecule fluorescence studies of IDPs and IDRs
PART II Molecular Mechanism 5. Experimental studies of binding of intrinsically disordered proteins to their partners 6. Modeling protein-protein interactions with intrinsically disordered proteins
PART III Biology and Medicine 7. IDPs and IDRs in biomolecular condensates 8. Molecular mechanisms of fibrillation of IDPs 9. Perspectives on drug discovery strategies based on IDPs 10. Conclusion and future directions
