Structure and Intrinsic Disorder in Enzymology. Foundations and Frontiers in Enzymology

Table of Contents

1. Enzymology: Early insights 2. Deep mutational scanning to probe specificity determinants. 3. Protein flexibility and cryo-enzymology: The trade-off between stability andcatalytic rates 4. Thermodynamic Perspective of Protein Disorder and Phase Separation: Model Systems 5. Structure and disorder: Protein functions depend on this new binary transforming lock-and-key into structure-function continuum 6. Methods for measuring structural disorder in proteins 7. Prediction of protein structure and intrinsic disorder in the era of deep learning 8. Roles of Intrinsically Disordered Regions in Phosphoinositide 3-Kinase Biocatalysis 9. Many faces of protein promiscuity: Not just broad specificity of proteins 10. Role Of Plasticity And Disorder In Protein Moonlighting: Blurring Of Lines Between Biocatalysts And Other Biologically Active Proteins 11. Molten globular enzymes 12. Intrinsic disorder and allosteric regulation 13. Macromolecular Crowding: How it Affects Protein Structure, Disorder, and Catalysis 14. Intrinsic disorder and post-translational modifications: An evolutionary perspective 15. The roles of prion-like domains in amyloid formation, phase separation, and solubility 16. IDPRs of membrane proteins influence membrane curvature 17. How binding to surfaces affects disorder

Authors

Munishwar Nath Gupta Former Emeritus Professor, Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology, Delhi, India. 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 Professor, Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, Florida, USA. VLADIMIR N. UVERSKY is a Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF). He obtained his academic degrees from Moscow Institute of Physics and Technology (Ph.D., in 1991) and from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences (D.Sc., in 1998). He spent his early career working mostly on protein folding at the Institute of Protein Research and the Institute for Biological Instrumentation (Russia). In 1998, he moved to the University of California Santa Cruz where for six years he was studying protein folding, misfolding, protein conformation diseases, and protein intrinsic disorder phenomenon. In 2004, he was invited to join the Indiana University School of Medicine as a Senior Research Professor to work on the intrinsically disordered proteins. Since 2010, Professor Uversky is with USF, where he continues to study intrinsically disordered proteins and protein folding and misfolding processes. He has authored over 1150 scientific publications and edited several books and book series on protein structure, function, folding and misfolding. He has been listed as Highly Cited ResearchersT every year from 2014 to 2020. In 2021, he was elected as a Fellow of the Royal Society of Biology and a Fellow of the Royal Society of Chemistry. Professor Uversky collaborated with more than 12,500 colleagues from more than 2,750 research organizations in 89 countries/territories.