Protein Folding: Denatured<->Transition<->Native States Investigated with Experiment and Simulations

Friday, March 23, 2018

Dr. Tobin Sosnick

Biochemistry and Molecular Biology

University of Chicago

Hand 1144, 3:30 PMSosnick

Abstract:  I will present a broad view of the protein folding process, describing properties of denatured and intrinsically disordered proteins, the major folding events including rate limiting steps, and conclude with a presentation of our new Upside algorithm that is able to de novo fold proteins in cpu-days.

Bio:   Tobin R. Sosnick, Chair of the Dept. of Biochemistry & Molecular Biology, would be at home in either a chemistry or physics department, having received his PhD in low-temperature physics from Harvard University in 1988. His shift into biological research occurred during his post-doctoral training with the W. Englander (protein chemistry, NAS, UPenn) and J. Trewhella (biophysics, Los Alamos). Prof. Sosnick is a founding member of the Institute for Biophysical Dynamics, serving as its Director from 2009 to 2011, as well as a Senior Fellow in the Computation Institute. He has led the development and design of the Graduate Program in Biophysical Sciences.

Prof. Sosnick’s research program involves synergistic studies of protein and RNA folding, function and design, with both experimental and computational approaches. The research is based on the premise that rigorous and innovative studies of basic processes have broad implications in many areas of biological research. Research areas include delineating protein and RNA folding pathways and denatured states, ab initio protein folding pathway and structure prediction, design of light-triggered allosteric proteins, and protein-RNA interactions.

His lab employs a range of experimental and theoretical methods including NMR, small-angle X-ray scattering, hydrogen exchange, rapid mixing methods, molecular dynamics and coarse-grain folding simulations.

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