I am interested in how protein dynamics contribute to biological function. In my research group we primarily use nuclear magnetic resonance (NMR) spectroscopy to study protein dynamics over a wide range of time scales, from picoseconds to seconds. We address specific questions regarding the role of protein dynamics in various types of function and dysfunction, for example: ligand binding and allostery, enzyme catalysis, and protein misfolding and aggregation. To achieve this, we develop new NMR methods and often interpret the results in combination with molecular dynamics simulations.

Our research has resulted in unique insights showing how conformational entropy can contribute significantly to ligand binding and allostery, which has future applications in the field of drug design.  Another key result is the critical role of rare, transient, high-energy conformations in biological function: proteins spontaneously undergo transitions between multiple structural states that are either active or inactive. These types of transitions can mediate allosteric signaling within proteins via distinct pathways that we have detected using NMR spectroscopy.