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DEPARTMENT of BIOLOGY Vladimir Uversky University of Southern Florida, Tampa “Intrinsic Disorder and Protein Structure-Function Continuum”

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DEPARTMENT of BIOLOGY Vladimir Uversky University of Southern Florida, Tampa “Intrinsic Disorder and Protein Structure-Function Continuum” B DEPARTMENT OF BIOLOGY Vladimir Uversky University of Southern FloridA, Tampa “Intrinsic disorder and protein structure-function continuum” Friday, March 24, 2017 12:00 PM Chao Auditorium, Ekstrom Library Background: Proteins are often imagined as globular arrangements of polypeptides with well-defined, ordered structures and active sites that define and regulate their functions. This model of protein structure and function, termed the ‘lock and key’ model, explains the function of many proteins, but does not account for the growing population of proteins that lack well-defined secondary and tertiary structure motives, termed intrinsically disordered proteins (IDP). IDPs, unlike ordered, globular proteins, natively exhibit very little defined structure as a critical contributor to their function. The conformational plasticity of these proteins allows for specialized one- to-many interactions that are useful for regulation, molecular exclusion by force repulsion such as found at nuclear pores, or a growing number of other functionalities still being discovered. Furthermore, proteins may exist in intermediate forms. Rather than being strictly ordered or disordered, proteins may be partly disordered (molten globules), partly ordered (pre-molten globule), or have regions of intrinsic disorder that function as linkers, spacers, or post translational modification sites. Proteins, based on their environment, may transition between these different conformations resulting in activation or deactivation which may be either reversible or permanent. Figure 1: The Protein Structure Continuum (modified after References to Recent Papers and Related Uversky, V. 2002. Protein Sciences 11 (4):739-56). Reviews: (1) Uversky, V. 2016. Dancing Protein Clouds: The Strange Biology and Chaotic Physics of Intrinsically Disordered Proteins. Journal of Biological Chemistry 291 (13): 6681 – 6688. (2) Uversky, V. 2016. Protein Intrinsic Disorder-Based Liquid-Liquid Phase Transitions in Biological Systems: Complex coacervates and membrane-less organelles. Advances in Colloid and Interface Science 239: 97 – 114. (3) Deforte, S. and Uversky, V. 2016. Order, Disorder, and Everything in Between. Molecules 21(8): 1090. (4) Uversky V. 2015. Protein Misfolding in Lipid-Mimetic Environments. Advances in Experimental Medicine and Biology 855: 33-66, (5) Uversky, V. 2014. Introduction to Intrinsically Disordered Proteins (IDPs). Chemicals Reviews 114 (13): 6557 – 6560. Dr. Vladimir Uversky Dr. Uversky is an Associate Professor in the Department of Molecular Medicine at the University of Southern Florida. He earned his PhD in Biophysics from the Moscow Institute of Physics and Technology in 1991 and his DSc in Biophysics from the Institute of Experimental and Theoretical Biophysics in 1998. Dr. Uversky has published over 550 scientific papers regarding protein folding and misfolding, has edited eight different books on intrinsically disordered proteins in addition to five book series, is an editor on several journals and serves as the executive editor for the journal Intrinsically Disordered Proteins. Dr. Uversky uses a combination of experimental and bioinformatics approaches to elucidate the folding behavior and functions of intrinsically disordered proteins in the light of pharmaceutical biophysics. To accomplish this, Dr. Uversky values collaboration and team-based research. To date, he has worked on over 100 collaborative projects with partners from 16 different countries. HONORS, AWARDS, AND PROFESSIONAL RECOGNITION: 1990. Fellowship from the Biochemical Society of UK. 1992. Premium of Academiae Europaeae for Young Russian Scientists. 1992. Soros Individual Award. 1993. Soros Award for Advanced Scientist. 1998-1999. Fellowship from Parkinson Institute. 1994, 1995, 1996 and 1997. Fellowships from Federal Ministry of Education, Research and Technology (BMBF, Germany). 2007. Outstanding Academic Service Award. IEEE 7th International Conference on Bioinformatics and BioEngineering. 2008. Outstanding Achievement Award. WORLDCOMP’08. 2012. F1000 Faculty Member of the Year 2012 in Structural Biology. 2013. F1000 Faculty Member of the Year 2013 in Structural Biology. 2014. 2014 Thomson Reuters Highly Cited Researcher. 2014. The World’s Most Influential Scientific Minds: 2014 .
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