J Patrick Loria

J Patrick Loria's picture
Professor of Chemistry and of Molecular Biophysics and Biochemistry
225 Prospect St, New Haven, CT 06511-8499
203 436 2518

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

Recent Publications

S. K. Whittier, A. Hengge, & J. P. Loria. Conformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases. Science 2013, 341, 899-903.

J. Lipchock, H. Hendrickson, B. Douglas, K. Birg, P. Ginther, I. Rivalta, N. Ten, V. Batista, & J. P. Loria. Characterization of PTP1B inhibition by chlorogenic and cichoric acid. Biochemistry 2016, 56, 96-106.

I. Rivalta, G. P. Lisi, N.-S. Snoeberger, G. A. Manley, J. P. Loria, & V. S. Batista. Allosteric communication disrupted by a small molecule binding to the imidazole glycerol phosphate synthase protein-protein interface. Biochemistry 2016, 55, 6484-6494.

G. P. Lisi, G. A. Manley, H. Hendrickson, I. Rivalta, V. S. Batista, & J. P. Loria. Dissecting dynamic allosteric pathways using chemically related small molecule activators. Structure 2016, 24, 1155-1166.

B. Moscato, M. Swain, & J. P. Loria. Induced fit in the selection of correct versus incorrect nucleotides by DNA polymerase beta. Biochemistry 2016, 55, 382-395.

G. P. Lisi and J. P. Loria. Solution NMR spectroscopy for the study of enzyme allostery. Chem. Rev. 2016, 116, 6323-6369.

Research Interests

Room Number: 
KCL 115