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 12/05/2017

John Skinner

Congratulations to John Skinner and our collaborators in the Rosner lab on having their paper, entitled "Conserved salt-bridge competition triggered by phosphorylation regulates the protein interactome", published in PNAS.

Welcome 11/1/2017

sosnick

Welcome to Ruofen Chen, who is joining our group as an IME graduate student

In the news... 10/13/2017

Joshua RibackAdam ZmyslowskiJohn Jumper

Our work on disordered proteins in solution has been featured on UChicago News, Notre Dame News, and News Medical. Congratulations to Josh Riback, Adam Zmyslowski, John Jumper, and our collaborators in the Clark and Drummond labs.

Paper Published 10/12/2017

Joshua RibackAdam ZmyslowskiJohn Jumper

Congratulations to Josh Riback, Adam Zmyslowski, John Jumper, and our collaborators in the Clark lab at the University of Notre Dame and the Drummond lab on having their paper, entitled "Innovative scattering analysis shows hydrophobic disordered proteins are expanded in water," published in Science!

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 Early Edition

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