Area of interest
Protein dynamics, allosteric function, structural biology, NMR spectroscopy.
Nearly all biological processes are driven by the same fundamental event: protein conformational changes. The mechanics that govern how proteins “morph” their three-dimensional structures into alternative conformations need to be understood in order to understand the biochemical basis of protein function. Our research is aimed at atomic resolution characterizations of the structural and dynamic properties of proteins and their interactions with other proteins, ligands, and small molecule drugs. Towards this goal, we are making extensive use of heteronuclear NMR spectroscopy and other experimental and theoretical tools. NMR spectroscopy is ideal for our studies, as hundreds – even thousands – of structural and motional “spin probes” are uniformly distributed throughout any given protein. We have a general interest in the role of dynamics in protein function and allostery.
Awards and Honors
- 2006 Junior Faculty IBM Fund Award
- 2001-2002 American Association of Colleges of Pharmacy (AACP) New Investigators Program (NIP) Award for Pharmacy Faculty: University of North Carolina at Chapel Hill.