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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.


Unifies the roles of intrinsic disorder and structure in the functioning of enzymes and proteins
Examines a range of enzyme and protein characteristics, their relationship to intrinsic disorder, and methods for study
Features chapter contributions from international leaders in the field

-도서목차-

1. Enzymology: Early insights
Dr M N Gupta, Former Emeritus Prof, IIT Delhi, India
2. Decoding the twin magics of fast rates and specificity
Prof Yakov Levy, Dept of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel
3. Protein flexibility and cryo-enzymology: The trade-off between stability and catalytic rates
Prof Emeritus George N Somero, Hopkins Marine Station, Stanford University, USA
4. Structure and Disorder: Functions depend upon this new binary
Prof V.N.Uversky
5. Hierarchies of intrinsic disorder
Prof V.N.Uversky
6. Methods for measurement of disorder in proteins
Dr Nathalie Sibille, Centre for Biochemical Structures, Univ of Montpellier, France
7. Bioinformatics tools for predictions of structure, disorder, and function
Dr Zsuzsanna Dosztányi, Dept of Biochemistry, Eotvos Lorand Univ, 1117 Budapest, Hungary
8. How do new enzyme activities evolve ? [The relatively recent ideas on de novo genes to be included apart from the role of intrinsic disorder and promiscuity]
Dr Claudio Casola, Dept of Ecology and Conservation, Texas A & M University, Texas 77843, USA
9. Emerging role of Intrinsic disorder in biocatalysis
Dr Shelly DeForte, Dept of Molecular Medicine,Univ of South Florida, Florida, 33612, USA
10. Role of disorder in protein promiscuity
Dr Shoshana J Wodak, Virje Univ Brussel 1050 Brussel, Belgium
11. Role of disorder in protein moonlighting
Prof Peter Tompa, Institute of Enzymology Hungarian Academy of Sciences, 1113, Budapest, Hungary
12. Molten globular enzymes
Donald Hilvert Laboratory of Organic Chemistry, ETH Zurich, CH-8093 Zurich, Switzerland
13. Intrinsic disorder and allosteric regulation
Prof Zhirog Liu, College of Chemistry and Molecular Engineering, Peking Univ, Beijing, China
OR Prof Vincent Hilser ,Dept of Biology, Johns Hopkins, Baltimore, MD 21218-2685, USA
14. Protein crowding: How it affects structure, disorder and catalysis
Prof Benjamin Schuler, Dept of Biochemistry, Univ of Zurich, 8057, Zurich, Switzerland
15. How structure and disorder affect each other?
Prof B. Montgomery Pettitt, Centre of Structural Biology and Mol Biophysics Univ of Texas Medical Branch, Galvaston 77555,Texas, USA
16. Role of disorder in post-translational modifications
Paul M Harrison, Dept of biology, McGill Univ., Canada
17. Structure, Intrinsic disorder and protein misfolding/aggregation
Prof Hidekazu Hiroaki, Dept of Basic Medical Sciences, Nagoya University, Japan
18. Intrinsic disorder, amyloids and prion-like domains in proteins.
Prof Salvador Ventura,Dept of Biochemistry and Molecular Biol, Univ of Barcelona, 08193, Balaterra [Barcelona], Spain
19. IDPRs of membrane proteins influence membrane curvature
Prof M.A.E. Claessens, Faculty of Science and Technology, Univ of Twente,Enshede,7522 NB, The Netherlands
20. How binding to surfaces affects disorder?
Prof Rafael Bruschweiler, Dept of Chemistry and Biochemistry, The Ohio State Univ., Columbus, Ohio,OH 43210, USA
21. Intrinsic disorder, phase separation and membrane-less cellular organelles
Prof V N Uversky


-About the Editors-

Munishwar Gupta

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.
Affiliations and Expertise
Former Emeritus Professor, Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology, Delhi, India

Vladimir Uversky

Dr. Uversky received B.S. and M.S. degrees in Physics from Leningrad State University in Russia in 1986, then, completed Ph.D. and Doctor of Sciences (D.Sc.) degrees in Physics and Mathematics (field of study - Biophysics) at the Moscow Institute of Physics and Technology (1991) and the Institute Experimental and Theoretical Biophysics of the Russian Academy of Sciences (1998), respectively. In 1998, he moved to the University of California Santa Cruz to study protein folding, misfolding, protein conformation diseases, and protein intrinsic disorder phenomenon. In 2004, he was invited to join the Indiana University School of Medicine to primary work on the intrinsically disordered proteins, and since 2010 has been on faculty at the University of South Florida. He has authored over 850 scientific publications and edited several books and book series on protein structure, function, folding and misfolding. He is an editor of several scientific journals.
Affiliations and Expertise
Professor, Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, Florida, USA

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