Faculty

My research focuses on the broad question of how the sequence of a protein determines its particular three-dimensional structure, along with its dynamic and functional properties. Part of our effort in structural biology is aimed at developing new technology for nuclear magnetic resonance (NMR) spectroscopy that will allow us to determine validated structures more quickly and at lower cost. A still wider view is provided by systems biology, which seeks to explain the interactions of all cellular components. Our particular interest is in metabolomics, where we are developing technologies for identifying and quantifying, in high-throughput fashion, the major metabolites in tissues and biological fluids so as to be able to compare them with the genomic, proteomic, and environmental state of the organism. We use NMR spectroscopy for high-throughput screening of ligands that bind to biological macromolecules as the means for identifying functions of unknown proteins or for discovering how small molecules affect functional properties of proteins. We also maintain the Biological Magnetic Resonance data Bank (BMRB), which archives information on proteins, nucleic acids, natural products, and metabolites, and serves as one of the four partner sites of the Worldwide Protein Data Bank.