Our research is directed towards an understanding of non-covalent interactions in chemical and biochemical systems. We employ a variety of techniques in our work, but nuclear magnetic resonance is our most important tool. NMR can be used to obtain structures of complex macromolecules and is sensitive to molecular dynamics over a wide range of time scales. Equally important is the ability of NMR to provide information concerning intermolecular interactions via nuclear Overhauser effects. Combining NMR with other experimental and computational methods, we are actively investigating the following areas:

Cytochrome P450 structure and dynamics

Methods for characterizing paramagnetic proteins by NMR

Enzymes in the methionine salvage pathway: structure and function

Closed-shell ion pair structure and dynamics

Amino acid interaction free energies for protein folding simulations: experimental and theoretical considerations


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