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Picture courtesy of
Center for Molecular Biophysics |
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Gaetano T. Montelione The general aim of our research is to use NMR spectroscopy as a tool for protein engineering and rational drug design. We develop new methods for protein solution structure determination and apply these techniques to proteins of pharmaceutical or medical interest. The combined techniques of site-directed mutagenesis, NMR spectroscopy, and conformational energy calculations are being used to (1) determine three dimensional structures of small proteins in solution, (2) determine the structures of protein-protein, protein-receptor, and protein-nucleic acid complexes, (3) characterize effects of amino acid substitutions on protein structure, stability, and dynamics, (4) direct efforts to design and engineer proteins and provide information for rational drug design, and (5) study the molecular mechanisms by which proteins fold into their biologically-active conformations. This research has important implications in the fields of protein physical chemistry, molecular design, receptor-ligand interactions, and oncogenesis.
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