Research Interests:

Solution NMR is a useful method to study protein structure and dynamics. Standard NMR experiments use protein uniformly labeled with NMR active nuclei, such as 15N, 13C and 2H.  Each nucleus reports on its surrounding environment and the ability to obtain structural information depends on being able to resolve, and unambiguously assign all resonance frequencies to unique nuclei. However, for large proteins (> 30 kDa) resonance overlap properties render this process difficult. My goal is to help develop NMR methods to study large proteins in solution. Towards this goal, I am applying selective labeling methods to study the structure and dynamics of the 118 kDa HIV-1 reverse transcriptase, a major drug target in the treatment of HIV-1 infection. The NMR spectra of RT produced by these labeling methods contain less resonance overlap since only a few residues are labeled.

Education: 

Chemistry (biochemistry track) University of North Carolina at Chapel Hill


PhD Advisor: Dr Angela Gronenborn


email: ngs10{AT} pitt.edu

Lab Address:

Department of Structural Biology


Publications:

Inventor in a provisional patent titled: Device for particulate NMR samples in a fluid.