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Intrinsically Disordered Proteins

  • ID: 4759527
  • Book
  • 355 Pages
  • Elsevier Science and Technology
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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.

  • Provides in-depth discussion of fundamental IDP and IDR dynamics, function, and binding, with mechanistic insight to support new drug development
  • Describes the role of new computational and experimental approaches in characterizing the binding of IDPs to their functional targets
  • Features chapter contributions from international experts in IDP and IDR biochemical function and methods of study

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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

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Salvi, Nicola
Dr. Nicola Salvi is a research scientist at the Institut de Biologie Structurale in Grenoble, France. After receiving his doctorate from the Ecole Polytechnique Fédérale de Lausanne, Switzerland, under the supervision of Geoffrey Bodenhausen, he held a postdoctoral appointment at Harvard Medical School. Dr. Salvi is an expert in characterizing protein dynamics using nuclear magnetic resonance spectroscopy. He developed hybrid approaches in which spectroscopic evidence on intrinsically disordered proteins (IDPs) is combined with molecular dynamics simulation to obtain insights into the functional dynamics of IDPs. Dr. Salvi's studies led to identifying mechanistic paradigms of IDP motions, with important implications for our understanding of their function.
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