Date/Time
Date(s) - 04/01/2024
3:00 pm - 4:00 pm
Location
Communicore, C1-11
Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structure under physiological conditions in vitro. IDPs are characterized by an astonishing multi-level spatiotemporal heterogeneity, with their mosaic structure representing a complex combination of foldons, inducible foldons, morphing inducible foldons, non-foldons, semi-foldons, and unfoldons.
IDPs are highly abundant in nature and have functional repertoire that is very broad and complements functions of ordered proteins. Often, IDPs are involved in regulation, signaling and control pathways, commonly acting as hubs in protein-protein interaction networks. Intrinsic disorder is an important constituent of the proteoform concept, representing one of the important means of functional diversification of the proteinaceous products of a gene. Functions of IDPs may arise from specific disordered forms, from inter-conversion of disordered forms, or from order ↔ disorder transitions. The choice between these conformations is determined by the peculiarities of the protein environment, and many IDPs possess an exceptional ability to differently fold in a template-dependent manner. As a result, many IDPs are capable of conducting multiple functions, with such multifunctionality being linked to their spatiotemporal heterogeneity. Therefore, a correlation between protein structure and function represents a “protein structure–function continuum”, where a given protein exists as a dynamic conformational ensemble containing multiple proteoforms characterized by diverse structural features and miscellaneous functions.
Bio:
Vladimir N. Uversky, B.S., M.S., Ph.D., D.Sc., Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida. He received 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. Dr. Uversky has authored over 1250 scientific publications. According to the Thomson Reuters’ Web of Science, his work was cited more than 70,900 times, and he has an H-index of 128. Dr. Uversky has been included in the prestigious Clarivate list of Highly Cited Researchers™ every year from 2014 to 2020. In 2021, he was elected as a Fellow of the Royal Society of Biology and a Fellow of the Royal Society of Chemistry. Over the years, he delivered more than 250 invited talks at various national and international conferences and invited seminars in various universities and research institutions around the globe. Dr. Uversky collaborated with more than 12,500 colleagues from more than 2,750 research organizations in 89 countries/territories. He is an editor of a number of scientific journals and edited several books and book series on protein structure, function, folding and misfolding.
IDPs are tightly controlled in the norm by various genetic and non-genetic mechanisms. Alteration in regulation of this disordered regulators are often detrimental to a cell, and many IDPs are associated with a variety of human diseases, such as cancer, cardiovascular disease, amyloidoses, neurodegenerative diseases, diabetes and others. Furthermore, many IDPs are multipathogenic, being associated with the origination and development of a number of different diseases. Therefore, there is a though-provoking interconnection between intrinsic disorder, cell signaling, and human diseases, with polypathogenicity of the involved proteins being linked to their structural plasticity and multifunctionality.