Research Interests

We currently study protein folding, protein structure/function relationships, protein-protein interactions and the mechanisms of enzymatic reactions. The long-term goal of the protein folding work is to understand the nature of the intermediate structures on the unfolding and refolding pathways, including the role of proteins that assist folding (particularly the bacterial chaperone, GroEl). The work uses site-directed mutagenesis and techniques such as equilibrium and stopped-flow 19F and proton NMR, circular dichroism, fluorescence measurements and x-ray crystallography. Proteins in these studies include the intestinal fatty acid binding protein, dihydrofolate reductase and actin. Studies on protein-protein interactions are related to the folding studies but also include actin, actin binding proteins and polymerization processes. The long-term goal of this work is to understand the role of actin in maintaining the cytoskeletal structure of cells and how such structures control cellular functions. Studies on site-directed mutants of actin are underway. While kinetic simulation and fitting programs have been developed, the long-term goal of kinetic studies with enzymes is to understand the catalytic mechanism of specific enzymatic reactions.

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Primary Section

Section 29: Biophysics and Computational Biology

Secondary Section

Section 21: Biochemistry