Professor of Chemistry
Professor of Molecular Biophysics and Biochemistry
Member of Yale faculty since 2001
Research Flexibility is an integral part of enzyme function. This conformational motion can include reorganization of catalytic groups, loop closures, and domain movements, to name a few. In enzymes these motions are often the rate-determining step in the catalytic process. Their characterization is therefore crucial to understanding enzyme function, for optimizing catalysts, for understanding protein-ligand interactions, and for de novo enzyme design. The focus of our research is to understand how the dynamic and structural properties of proteins correlate with their function with particular emphasis on enzymes and allosterism.
Our primary experimental tool for addressing these questions is solution nuclear magnetic resonance (NMR) spectroscopy, which allows quantitative, atomic-resolution insight into the kinetics, thermodynamics, and mechanism these important enzyme motions.
B.S. George Washington University, 1990
Ph.D. University of Notre Dame, 1997
NIH Postdoctoral Fellow-Columbia University, 1997-2001
Camille and Henry Dreyfus New Faculty award, 2001
NSF CAREER Award, 2003
Alfred P. Sloan Fellow, 2004
E.L. Kovrigin & J.P. Loria. Characterization of the transition state of functional enzyme dynamics. J Am Chem Soc. 2006, 128, 7724-5.
R.B. Berlow, T.I. Igumenova, & J.P. Loria. Value of a hydrogen bond in triosephosphate isomerase loop motion. Biochemistry 2007, 46, 6001-10.
E.D. Watt, H. Shimada, E.L. Kovrigin, & J.P. Loria. The mechanism of rate-limiting motions in enzyme function. Proc Natl Acad Sci U S A. 2007, 104, 11981-6.
J.M. Lipchock & J.P. Loria. 1H, 15N and 13C resonance assignment of imidazole glycerol phosphate (IGP) synthase protein HisF from Thermotoga maritime. J. Biomol. NMR Assign. 2008, 2, 219-21.
J.P. Loria, R.B. Berlow, & E.D. Watt. Characterization of enzyme motions by solution NMR relaxation dispersion. Acc Chem Res. 2008, 41, 214-21.