Our
laboratory strives to improve understanding of human pathology at a
molecular level. We utilize a combination of NMR spectroscopy, other
biophsycial techniques, and cell-based assays to describe how the
tertiary structures and thermodynamic behaviors of aqueous proteins determine their physiologic function. Important molecular characterizations include dynamic
conformational fluctuations, static structural stabilities, protein
surface electrostatics, ligand-binding and protein-protein assocation
reactions, all of which serve as the physico-chemical "toolkit" to
create the activities of biological life.
Protein systems that we are currently or have previously studied:
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