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.
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Dr. Munishwar Nath Gupta earned his PhD from Indian Institute of Science, Bengaluru, and completed post-doctoral positions at Massachusetts Institute of Technology (USA), University of Minnesota (USA), Lund University (Sweden), and University of Technology of Compiegne (France). He has taught chemistry, biochemistry, and biotechnology at the Indian Institute of Technology, Delhi, between 1975-2016. He was awarded the National Science Talent fellowship (India) and Fellowships of National Academy of Sciences and Indian National Science Academy. He has edited three books on thermostability of enzymes, non-aqueous enzymology and affinity-based separation methods. He was an Associate Editor of Biocatalysis and Biotransformation (Taylor and Francis) and the founding and former editor-in-chief of Sustainable Chemical Processes (Springer). He’s served on editorial boards of several national and international journals and acted as a consultant to Novozyme (Denmark), Dabur (India), and other international companies.
Vladimir N. Uversky is Professor in the Department of Molecular Medicine at the Morsani College of Medicine, University of South Florida. His research centers on protein folding, misfolding, and intrinsic disorder. He began his career at the Institute of Protein Research and the Institute for Biological Instrumentation in Russia, before moving to the University of California, Santa Cruz in 1998 and Indiana University–Purdue University Indianapolis in 2004, where he served as Senior Research Professor. He has been at USF since 2010 and is a Fellow of the Royal Society of Biology, the Royal Society of Chemistry, the American Institute for Medical and Biological Engineering, and the American Association for the Advancement of Science. Professor Uversky has authored numerous research papers and reviews and edited several books and book series on protein structure, folding, and misfolding. He serves as an editor for several scientific journals.
For more than a 100 years, the structure-function relationship has been a cornerstone of biology. However, it has recently emerged that intrinsic disorder is as important as well-defined structures for protein and enzyme function.
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 modifications; protein misfolding and aggregation; myloids and prion-like domains; and phase separation in membrane-less cellular organelles, among other topics. Chapters also review methods for study, as well as evolving technology to support new research across academic, industrial, and pharmaceutical labs.
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