Tobin R. Sosnick
My research program involves synergistic studies of protein and RNA folding, function and design, with both experimental and computational components. The research is based on the premise that rigorous and innovative studies of basic processes have broad implications in many areas of biological research. My experimental experience in protein folding, design, modeling, and biophysical methods provides an enormous benefit to our computational studies which heavily rely on the use of fundamental principles of protein folding. Since my Ph.D. in low temperature physics in 1989, I have entered many different biological fields and have made an impact in each area. These areas include delineating protein and RNA folding pathways, de novo structure prediction, design of light-triggered allosteric proteins, and RNA folding during transcription. My lab employs a range of experimental and computational methods including NMR, small-angle X-ray scattering, rapid mixing methods, hydrogen exchange, molecular dynamics and coarse-grain folding simulations. I am a very a strong believer in collaboration, having co-mentored 15+ students and post-doctoral fellows who produced 30+ papers in the last 10 years.
The folding of single domain proteins: have we reached a consensus? Sosnick, T.R., Barrick, D.(2010) Curr. Opin. Struct. Biol.
A discrete structure of an RNA folding intermediate revealed by cryo-electron microscopy. Baird, N. J., Ludtke, S.J., Khant, H., Chiu, W., Pan, T., Sosnick, T.R. (2010) J. Amer. Chem. Soc. 132:16352-3
Modeling the Hydration Layer around Proteins: HyPred Virtanen, J.J. Makowski, L., Sosnick, T.R., Freed, K.R. (2010) Biophys. J. 95, 1611-9.
Rationally improving LOV domain-based photoswitches. Strickland, D., Yao, X., Gawlak, G., Rosen, M. K., Gardner, K. H., and Sosnick, T. R. (2010) Nature Meth. 7(8), 623-626.
Protein structure prediction enhanced with evolutionary diversity: SPEED. DeBartolo J, Hocky G, Wilde M, Xu J, Freed KF, Sosnick TR.(March 2010 Cover of Protein Science)
Protein vivisection reveals elusive intermediates in folding. Zheng Z, Sosnick TR.(Feb 2010) J Mol Biol.
Light-activated DNA binding in a designed allosteric protein. Strickland D, Moffat K, Sosnick TR. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10709-14. Epub 2008 Jul 30.
Fast folding of a helical protein initiated by the collision of unstructured chains. Meisner, W. K. & Sosnick, T. R., Proc. Natl. Acad. Sci. USA 101, 13478-82, 2004.