Research Departments & Organizations
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.
Specialized Terms: Protein Folding
Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase.
Wang Y, Berlow RB, Loria JP. Role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase. Biochemistry 2009, 48:4548-56. 2009
The mechanism of rate-limiting motions in enzyme function.
Watt ED, Shimada H, Kovrigin EL, Loria JP. The mechanism of rate-limiting motions in enzyme function. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104:11981-6. 2007