Intrinsically Disordered Proteins

Vladimir Uversky obtained his Ph.D. in biophysics from Moscow Institute of Physics and Technology (1991) and D.Sc. in biophysics from Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences (1998). He spent early career working on protein folding at Institute of Protein Research and the Institute for Biological Instrumentation (Russian Academy of Sciences). In 1998, he moved to the University of California Santa Cruz to work on protein folding, misfolding and protein intrinsic disorder. In 2004, he moved to the Center for Computational Biology and Bioinformatics at the Indiana University Purdue University Indianapolis to work on the intrinsically disordered proteins. Since 2010, he is with the Department of Molecular Biology at the University of South Florida.

Introducing the phenomenon of protein intrinsic disorder.- Peculiar amino acid sequences of soluble IDPs.- Natural abundance of IDPs/IDPRs.- Wavy evolution of intrinsic disorder: Reinventing the wheel.- Structural heterogeneity of IDPs: When almost everything is possible.- Typical functions of IDPs and IDPRs.- Binding promiscuity and multitude of the disorder-based binding modes.- IDPs/IDPRs in human diseases.- IDPs as potential drug targets.- Concluding remarks: Intrinsic disorder as a universal tool for solving protein mysteries and riddles.