Vladimir N. Uversky
Department of Molecular Medicine at the University of South Florida (USF)
I am an Associate Professor at the Department of Molecular Medicine at the University of South Florida (USF). I obtained my Ph.D. from Moscow Institute of Physics and Technology (1991) and D.Sc. from Institute of Experimental and Theoretical Biophysics (1998). I obtained pre- and postdoctoral training in Structural Biology, Biochemistry and Biophysics (1991-1998, Institute of Protein Research, Russian Academy of Sciences) and spent early career working on protein folding at Institute of Protein Research and the Institute for Biological Instrumentation (Russia). In 1998, I moved to the University of California Santa Cruz where for six years I was studying protein folding, misfolding, protein conformation diseases, and protein intrinsic disorder phenomenon. In 2004, I was invited to join the Indiana University School of Medicine as a Senior Research Professor to work on the intrinsically disordered proteins. Since 2010, I am with USF, where I continue to study intrinsically disordered proteins and protein folding and misfolding processes. I have authored over 550 scientific publications and edited several books and book series on protein structure, function, folding and misfolding. I am also an editor of several scientific journals. The current research interests of my lab are focused on protein physics. We are studying protein structure, stability, dynamics, function, folding, misfolding, and non-folding, and are trying to establish relationships between the protein sequence and function in the light of pharmaceutical biophysics. We are using a combination of experimental and bioinformatics approaches to describe structural properties, functions, dynamics, and conformational stability of different proteins; to characterize their partially folded states; to analyze the molecular mechanisms of their folding and misfolding; to quantify structural consequences of protein interaction with various binding partners; to evaluate structural consequences of protein posttranslational modifications; to understand the effect of various environmental factors on protein folding, misfolding and conformational stability; to uncover the relationship between protein structure, stability and pathogenesis of various protein conformation diseases. One special category of proteins in our studies is termed intrinsically disordered proteins, which have no rigid 3-dimensional structures under physiological conditions but possess vital biological functions. We are elaborating and applying various experimental and computational techniques and tools to identify and characterize these proteins. We are evaluating the abundance of these proteins in various proteomes and are analyzing their structural and functional repertoire. We are studying the biological functions of these proteins and their evolution. We are also looking for some correlations between the peculiarities of intrinsically disordered proteins/regions and pathogenesis of human diseases.