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, and the American Institute for Medical and Biological Engineering. Professor Uversky co-founded the Intrinsically Disordered Proteins Subgroup at the Biophysical Society and the Intrinsically Disordered Proteins Gordon Research Conference, and has edited several books and book series on protein structure, folding, and misfolding. He serves as an editor for several scientific journals.

• 1. Enzymology: Early insights2. Deep mutational scanning to probe specificity determinants.3. Protein flexibility and cryo-enzymology: The trade-off between stability andcatalytic rates4. Thermodynamic Perspective of Protein Disorder and Phase Separation: Model Systems5. Structure and disorder: Protein functions depend on this new binary transforming lock-and-key into structure-function continuum6. Methods for measuring structural disorder in proteins7. Prediction of protein structure and intrinsic disorder in the era of deep learning8. Roles of Intrinsically Disordered Regions in Phosphoinositide 3-Kinase Biocatalysis9. Many faces of protein promiscuity: Not just broad specificity of proteins10. Role Of Plasticity And Disorder In Protein Moonlighting: Blurring Of Lines Between Biocatalysts And Other Biologically Active Proteins11. Molten globular enzymes12. Intrinsic disorder and allosteric regulation13. Macromolecular Crowding: How it Affects Protein Structure, Disorder, and Catalysis14. Intrinsic disorder and post-translational modifications: An evolutionary perspective15. The roles of prion-like domains in amyloid formation, phase separation, and solubility16. IDPRs of membrane proteins influence membrane curvature17. How binding to surfaces affects disorder

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, and the American Institute for Medical and Biological Engineering. Professor Uversky co-founded the Intrinsically Disordered Proteins Subgroup at the Biophysical Society and the Intrinsically Disordered Proteins Gordon Research Conference, and has edited several books and book series on protein structure, folding, and misfolding. He serves as an editor for several scientific journals.

• 1. Enzymology: Early insights2. Deep mutational scanning to probe specificity determinants.3. Protein flexibility and cryo-enzymology: The trade-off between stability andcatalytic rates4. Thermodynamic Perspective of Protein Disorder and Phase Separation: Model Systems5. Structure and disorder: Protein functions depend on this new binary transforming lock-and-key into structure-function continuum6. Methods for measuring structural disorder in proteins7. Prediction of protein structure and intrinsic disorder in the era of deep learning8. Roles of Intrinsically Disordered Regions in Phosphoinositide 3-Kinase Biocatalysis9. Many faces of protein promiscuity: Not just broad specificity of proteins10. Role Of Plasticity And Disorder In Protein Moonlighting: Blurring Of Lines Between Biocatalysts And Other Biologically Active Proteins11. Molten globular enzymes12. Intrinsic disorder and allosteric regulation13. Macromolecular Crowding: How it Affects Protein Structure, Disorder, and Catalysis14. Intrinsic disorder and post-translational modifications: An evolutionary perspective15. The roles of prion-like domains in amyloid formation, phase separation, and solubility16. IDPRs of membrane proteins influence membrane curvature17. How binding to surfaces affects disorder

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, and the American Institute for Medical and Biological Engineering. Professor Uversky co-founded the Intrinsically Disordered Proteins Subgroup at the Biophysical Society and the Intrinsically Disordered Proteins Gordon Research Conference, and has edited several books and book series on protein structure, folding, and misfolding. He serves as an editor for several scientific journals.

• 1. Enzymology: Early insights2. Deep mutational scanning to probe specificity determinants.3. Protein flexibility and cryo-enzymology: The trade-off between stability andcatalytic rates4. Thermodynamic Perspective of Protein Disorder and Phase Separation: Model Systems5. Structure and disorder: Protein functions depend on this new binary transforming lock-and-key into structure-function continuum6. Methods for measuring structural disorder in proteins7. Prediction of protein structure and intrinsic disorder in the era of deep learning8. Roles of Intrinsically Disordered Regions in Phosphoinositide 3-Kinase Biocatalysis9. Many faces of protein promiscuity: Not just broad specificity of proteins10. Role Of Plasticity And Disorder In Protein Moonlighting: Blurring Of Lines Between Biocatalysts And Other Biologically Active Proteins11. Molten globular enzymes12. Intrinsic disorder and allosteric regulation13. Macromolecular Crowding: How it Affects Protein Structure, Disorder, and Catalysis14. Intrinsic disorder and post-translational modifications: An evolutionary perspective15. The roles of prion-like domains in amyloid formation, phase separation, and solubility16. IDPRs of membrane proteins influence membrane curvature17. How binding to surfaces affects disorder