Our research is in the general area of molecular biological physics. Conformational flexibility and dynamics of protein molecues is often the key connection between the structure of a protein and its biological function. We are developing analytical and computational approaches to understand the mechanisms controlling large-scale (main-chain) structural changes in proteins. Examples include protein folding, allostery, and conformational changes induced from interactions with molecular surfaces.

We use a variety of theoretical concepts from statistical mechanics of phase transitions, soft condensed matter physics, and physical chemistry. We aim to bridge the gap between analytical theory, simulation, and experimental measurements to understand structure, dynamics and function of biomolecules. For students, this effort provides truly interdisciplinary research experience at the interface between physics, chemistry, and biology.

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• Capillarity-like growth of protein folding nuclei, Proc. Natl. Acad. Sci. USA (2008).
• Inherent flexibility and protein function: the open/closed conformational transition of the N-terminal domain of calmodulin, J. Chem. Phys. 128, 205104 (2008).
• Excluded volume, local structural cooperativity, and the polymer physics of protein folding rates, Proc. Natl. Acad. Sci. USA 104, 10841--10846 (2007).
• Non-Gaussian Dynamics from a Simulation of a Short Peptide: Loop Closure rates and Effective Diffusion Coefficients, J. Chem. Phys. 118, 2381--2391 (2003).
• Speeding Molecular Recognition by Using the Folding Funnel: The Fly-casting Mechanism', Proc. Natl. Acad. Sci. USA 97, 8868--8873 (2000).