Intrinsically Disordered Proteins

  • ID: 4759527
  • Book
  • 328 Pages
  • Elsevier Science and Technology
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Intrinsically Disordered Proteins: Dynamics, Binding, and Function thoroughly examines the fundamental biochemical functions of IDPs and IDRs, including signaling, binding and regulation. The role of new mechanistic, computational and experimental approaches in IDP study are explored in-depth, along with methods for the characterization of IDP dynamics, models, simulations, mechanisms of IDP and IDR binding, and biological and medical implications. In addition, leading researchers in the field of IDPs and IDRs contribute chapters on IDP approaches little explored to-date, such as ensemble descriptions of IDPs and IDRs, single-molecule studies of IDPs and IDRs, IDPs and IDRs in membraneless organelles, and more.

  • Provides in-depth discussions on fundamental IDP and IDR dynamics, function, and binding, along with mechanistic insights that 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: Methods for the characterization of dynamics and binding of IDPs 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 studies of IDPs and IDRs

Part II: Models and mechanisms of IDP and IDR binding 5. Experimental studies of IDP binding 6. Computational models of IDP binding

Part III: Biological and medical implications of IDP binding 7. IDPs and IDRs in membraneless organelles 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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