Self-assembly of chemical and biological systems. Transient interactions in solution by NMR. NMR of soluble proteins. Protein stability and folding by NMR and mutagenesis.

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:

Enzymes in the methionine salvage pathway: structure and function Monooxygenase enzyme systems: structure and dynamics Closed-shell ion pair structure and dynamics Amino acid interaction free energies for protein folding simulations: experimental and theoretical considerations