The Sosnick Group at The University of Chicago


The Sosnick Group strives to characterize the general principles that guide protein folding and dynamics. We combine multiple experimental and computational approaches to characterize the behavior of proteins in diverse contexts


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SAXS analysis - collapsed or expanded

Given small angle X-ray scattering (SAXS) dataset for an intrinsically disordered protein (IDP), we have developed an analysis method that can determine both the dimension of the ensemble as well as the quality of the solvent (i.e. the extent of self-interactions in the IDP).

Protein Folding - the 70% Rule

We have found that for many small 2-state proteins, the rate-limiting step of folding - the transition state - has ~70% of the native topology, according to the relative contact order.

 

Molecular Dynamics on your laptop!

Wouldn't it be nice to have physically realistic MD trajectories of protein dynamics without needing cpu-weeks/months of simulations? We have developed an MD engine that can reversibly fold some proteins up to 97 amino acids in cpu-days without requiring the use of fragments, homology or evolution.

Paper Published 08/02/2018

Joshua RibackAdam Zmyslowski

A new paper, "Commonly-used FRET fluorophores promote collapse of an otherwise disordered protein." by Joshua Riback, Adam Zmyslowski, and our collaborators in the Clark and Plaxco groups has been published to biorxiv. Check out the latest contribution to the SAXS-FRET debate!

Welcome 06/18/2018

David Hynes

Welcome to David Hynes, who is joining our group as a Summer Researcher.

Ph.D. 06/13/2018

Joshua Riback

Congratulations to Joshua Riback on successfully defending his doctoral disseration!

F1000Prime Recommendation 05/17/2018

Joshua RibackAdam ZmyslowskiJohn Jumper

Congratulations to Joshua Riback, Adam Zmyslowski, John Jumper, and our collaborators the in Clark and Drummond labs on having their Science paper, entitled "Innovative scattering analysis shows hydrophobic disordered proteins are expanded in water," recommended in F1000prime

Protein Folding

Protein Folding

Predicting Folding Dynamics

Predicting Folding Dynamics

Photoswitchable allosteric proteins

Photoswitchable allosteric proteins

Membrane Proteins

Membrane Proteins

Psi analysis

Psi analysis

Conformational Entropy

Conformational Entropy

J.J. Skinner, S. Wang, J. Lee, C. Ong, R. Sommese, S. Sivaramakrishnan, W. Koelmel, M. Hirschbeck, H. Schindelin, C. Kisker, K. Lorenz, T.R. Sosnick, M.R. Rosner, "Conserved salt-bridge competition triggered by phosphorylation regulates the protein interactome." Proc Natl Acad Sci U S A 114 (2017) 13453-8.

J.R. Riback, M.A. Bowman, A.M. Zmyslowski, C.R. Knoverek, J.M. Jumper, J.R. Hinshaw, E.B. Haye, K.F. Freed, P.L. Clark, T.R. Sosnick, "Innovative scattering analysis shows hydrophobic disordered proteins are expanded in water" Science 358 (2017) 238-41.

J.A. Riback*, C.D. Katanski*, J.L. Kear-Scott, E.V. Pilipenko, A.E. Rojek, T.R. Sosnick, D.A. Drummond, "Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response" Cell 168 (2017) 1028-40.

***Recommended in F1000prime***

A.R. French, T.R. Sosnick, R.S. Rock, "Investigations of human myosin VI targeting using optogenetically controlled cargo loading" Proc Natl Acad Sci U S A 114 (2017) E1607-16.

***Recommended in "F1000prime".***

Z.P. Gates*, M.C. Baxa*, W. Yu, J.A. Riback, H. Li, B. Roux, S.B.H. Kent, T.R. Sosnick, "Perplexing cooperative folding and stability of a low-sequence complexity, polyproline 2 protein lacking a hydrophobic core" Proc Natl Acad Sci U S A 114 (2017) 2241-6.

***Recommended in F1000Prime***

University of Chicago
Biochemistry & Molecular Biophsyics
Biophysical Sciences
Institute for Molecular Engineering
Institute for Biophysical Dynamics