Our research is directed to the understanding of structure, dynamics and ultimately function and mechanism of biological systems at atomic-resolution, using nuclear magnetic resonance (NMR) spectroscopy and molecular biology methods. Specifically, we are interested in the development and applications of multidimensional NMR techniques, which enable the measurement of observables such as chemical shifts, nuclear spin relaxation rates and the magnitudes and relative orientations of spin-spin couplings, in solution and solid phase. These NMR observables yield site-specific information about three-dimensional molecular structure (internuclear distances, torsional angles and relative orientations of bond vectors) and molecular dynamics. Systems of current interest include peptides and proteins, which self-assemble into supramolecular aggregates and are associated with protein misfolding disorders, membrane-associated peptides and proteins, and macromolecular complexes.
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