SciLifeLab The Svedberg seminar series, Vladimir N. Uversky, Intrinsically disordered proteins
Monday, December 3
Vladimir N. Uversky
Department of Molecular Medicine, University of South Florida, Tampa, Florida 33612, USA;
Laboratory of New Methods in Biology, Institute for Biological Instrumentation of the Russian Academy of Sciences Pushchino, Moscow region 142290 Russia;
I received my Ph.D. degree in Physics and Mathematics (field of study – Biophysics) at Moscow Institute of Physics and Technology in 1991 and Doctor of Sciences (D.Sc.) degree in Physics and Mathematics (field of study – Biophysics) at the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences in 1998. Currently, I am an Associate Professor at the Department of Molecular Medicine of University of South Florida, College of Medicine, and a Leading Scientist at the Institute for Biological Instrumentation, Russian Academy of Sciences. My research interests are focused on protein physics, and I study protein structure, stability, dynamics, function, folding, misfolding, and non-folding, being especially excited by everything related to intrinsically disordered proteins.
Unusual Biophysics and Strange Biology of Intrinsic Disorder
Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structure under physiological conditions in vitro. IDPs are highly abundant in nature, characterized by high structural heterogeneity, and have functions that are complementary to functions of ordered proteins. IDPs are characterized by sequential, structural, and spatiotemporal heterogeneity, rough and relatively flat energy landscapes, ability to undergo both induced folding and induced unfolding, ability to interact specifically with structurally unrelated partners, ability to gain different structures at binding to different partners, and ability to keep essential amount of disorder even in the bound form. Extended IDPs possess “turned-out” response to the changes in their environment. The heterogeneous spatiotemporal structure of IDPs can be described as a set of foldons, inducible foldons, semi-foldons, and non-foldons. Finally, various proteinaceous membrane-less organelles (PMLOs) almost invariantly contain IDPs, suggesting that the formation of these phase-separated droplets is crucially dependent on intrinsic disorder.