J Patrick Loria
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
“Glutamine hydrolysis by imidazole glycerol phosphate synthase displays temperature dependent allosteric activation” George Lisi, Allen Currier, and J. Patrick Loria Frontiers in Molecular Biosciences In Press (2017). Supported by NIH GM 106121
“Allostery in enzyme catalysis” George Lisi and J. Patrick Loria Current Opinion in Structural Biology 47, 123-130 (2017). Supported by NIH GM 106121
“Leveraging reciprocity to identify and characterize unknown allosteric sites in protein tyrosine phosphatases” Danica S. Cui, Victor Beaumont, Patrick S. Ginther, James M. Lipchock, and J. Patrick Loria J. Mol. Biol. 429, 2360-2372 (2017). Supported by NSF MCB 1615415 and GM 112781
“Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activity” George Lisi, Kyle East, Victor Batista, and J. Patrick Loria PNAS 114, E3414-E3423 (2017).
“Exploring protein structure and dynamics through a project-oriented biochemistry laboratory module” James Lipchock, Patrick Ginther, Bonnie Douglas, Kelly Bird, and J. Patrick Loria Biochem. and Mol. Biol. Ed. DOI: 10.1002/bmb/21056 (2017).
“Characterization of PTP1B inhibition by chlorogenic and cichoric acid” James Lipchock, Heidi Hendrickson, Bonnie Douglas, Kelly Bird, Patrick Ginther, Ivan Rivalta, Nicholas Ten, Victor Batista, and J. Patrick Loria Biochemistry 56, 96-106 (2016). Supported by NSF MCB 1615415