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J. PATRICK LORIA

The fields of drug design, protein engineering, and de novo protein design all require a detailed understanding of the flexibility and three-dimensional structures of the molecules involved. Using a powerful combination of solution NMR spectroscopy and biophysical methods the interplay between structure and motion and their impact on biological function are being determined for several enzymes. We are focusing on understanding the physical basis of allostery using the nezymes Imidazole glycerol phosphate synthase and tRNaseZ. The physico-chemical mechanism of protein motions in enzyme catalysis is being investigated in the enzymes triosephosphate isomerase and RNaseA.  Our ultimate goal is to provide a more complete picture of protein function that incorporates structure as well as important time-dependent motions.

Selected Publications

Watt, E., Shimada, H., Kovrigin, E. and Loria, J. P. The mechanism of rate-limiting enzyme motions. Proc. Natl. Acad. Sci. USA 104, 11981-11986 (2007)

Loria, J. P., Watt, E. and Berlow, R. B. Characterization of enzyme motions by solution NMR relaxation dispersion. Acc. Chem. Res. 41,214-221 (2008)

Wang, Y., Berlow, R. B. and Loria, J. P. The role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase. Biochemistry 48, 4548-4556 (2009)

Lipchock, J. M. and Loria, J. P. Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima. J. Biomol. NMR 45, 73-84 (2009)

Doucet, N., Watt, E. D. and Loria, J. P. The flexibility of a distant loop modulates motion and product release in ribonuclease A. Biochemistry 48, 7160-7168 (2009)

Last Updated 01-25-10