Flexibility of proteins is an integral part of their function. This motion can include reorganization of catalytic groups, loop closures, and domain movement, to name a few. The focus of our research is to understand how the dynamic and structural properties of proteins correlate with their function. Our primary experimental tool for approaching these questions is nuclear magnetic resonance (NMR) spectroscopy. NMR is the only experimental technique that can access molecular motion on time scales from 10^-12 - 10^1 seconds. Historically, detailed NMR studies have been restricted to peptides and small proteins. However recent advances in the field have allowed for in-depth studies of larger proteins, opening up this technique to a broad range of interesting protein dynamics questions.
- Wang, Y., Berlow, R., and J.P. Loria. (2009). The role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase Biochemistry. 48,4548-4556.
- Eric D. Watt, Hiroko Shimada, Evgenii L. Kovrigin, and J.P. Loria. (2007). The Mechanism of Rate-limiting Motions in Enzyme Function. PNAS 104, 11981-11986.