Current Fellows

With the burgeoning of research into the proteome over the past decade, our knowledge of the structure and function of individual proteins has become increasingly exhaustive. Markedly less exhaustive is our knowledge of how proteins function as they do in vivo — in the presence of a profusion of other biomolecules at high concentrations. In such dense environments, folding and complexation become highly frustrated, leading proteins to explore regions of their conformation space not expected on the basis of their crystal structures alone, thereby fundamentally altering their anticipated function.

Past work using Go-like lattice models has illustrated that in environments crowded by polymers or other proteins, folding is influenced just as strongly by entropy as by potential energy. Excluded volume effects can bias proteins toward folding and complexation along alternative pathways, or preclude folding and complexation altogether. In the future, I hope to extend these seminal efforts toward even more crowded membrane protein environments, where both experimental and computational techniques have, to date, fallen short. Of key interest is determining the precise physical role of membrane lipids in stabilizing membrane self-assembly processes in the absence of ligands. Equally crucial is the development of new physical and computational methods to facilitate further research. In such cramped environments, Monte Carlo techniques largely fail, necessitating the evolution of more advanced statistical and computational approaches.

Another recurring theme of my research is the ultrafast dynamics of liquids and glasses. Recent theoretical work in this arena has inspired new spectroscopic techniques for observing axially-symmetric liquid crystal systems, while future work will focus upon developing formalism to better understand glassy dynamics.