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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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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