J. Patrick Loria

Professor: Depts of Chemistry and Molecular Biophysics and Biochemistry

B.S. The George Washington University, 1990; Ph.D. University of Notre Dame, 1997; NIH Postdoctoral Fellowship, Columbia University, 1998-2000; joined Yale faculty 2001; Camille & Henry Dreyfus New Faculty Fellow; NSF CAREER 2003; Alfred P. Sloan Fellow 2004.

Selected References

• "Helix stabilization precedes aqueous and bilayer catalyzed fiber formation in islet amyloid polypeptide", Jessica A. Williamson, J.P. Loria and A.D. Miranker J. Mol. Biol.. In Press (2009).
• "The flexibility of a distant loop modulates active-site motion and product release in ribonuclease A", Nicolas Doucet, Eric Watt and J.P. Loria Biochemistry. 48,7160-7168 (2009).
• "Millisecond dynamics in the allosteric enzyme imidazole glycerol phosphate synthase (IGPS) from Thermotoga maritima", James Lipchock and J.P. Loria J. Biomol NMR. 45,73-84 (2009).
• "The role of loop-loop interactions in coordinating motions and enzymatic function in triosephosphate isomerase" Wang, Y., Berlow, R., and J.P. Loria Biochemistry. 48,4548-4556 (2009).
• "Molecular Interactions by NMR," James Lipchock and J.P. Loria in Methods Mol Biol:Protein Structure, Stability, and Interactions Humana Press (2009).
• "Characterization of enzyme motions by solution NMR relaxation dispersion," J.P. Loria, Rebecca B. Berlow, and Eric D. Watt Acc. Chem. Res. 41,214-221 (2008).
• "1H, 15N and 13C resonance assignment of imidazole glycerol phosphate (IGP) synthase protein HisF from Thermotoga maritima," James Lipchock and J.P. Loria Biomol. NMR Ass. 2,219-221 (2008).
• "The Mechanism of Rate-limiting Motions in Enzyme Function," Eric D. Watt, Hiroko Shimada, Evgenii L. Kovrigin, and J.P. Loria PNAS 104, 11981-11986 (2007).
• "The value of a hydrogen bond in triosephosphate isomerase loop motion," R. Berlow, T. Igumenova, and J.P. Loria Biochemistry 46, 6001-6010 (2007).
• "Solution structure of an rRNA substrate bound to the pseudouridylation pocket of a box H/ACA snoRNA," Hong Jin, J.P. Loria, and Peter B. Moore Mol. Cell 26, 205-215 (2007).
• "Dynamic requirements for a functional protein hinge," Kempf, J.G., Jung, J., Ragain, C., Sampson, N., and J.P. Loria J. Mol. Bio. 368, 131-149 (2007).
• "The effects of cosolutes on protein dynamics: The reversal of denaturant-induced protein fluctuations by trimethylamine N-oxide," Vicky Doan-Nguyen and J.P. Loria Protein Science 16,20-29 (2007).
• "Crystallization and characterization of the thallium-form of the Oxytricha nova G-quadruplex," Michelle Gill, Scott Strobel and J.P. Loria Nuc. Acid Res. 34, 4506-4514 (2006).
• "Characterization of the transition state of functional enzyme dynamics," Evgenii L. Kovrigin and J.P. Loria J. Am. Chem. Soc. 128,7724-7725 (2006).
• "Enzyme dynamics along the reaction coordinate: critical role of a conserved residue," Evgenii L. Kovrigin and J.P. Loria Biochemistry 45,2636-2647 (2006).
• "Faithful estimation of dynamics parameters from CPMG relaxation dispersion measurements," Evgenii L. Kovrigin, James G. Kempf, Michael J. Grey, and J.P. Loria J. Magn. Reson. 180,93-104 (2006).
• "205Tl NMR methods for the characterization of monovalent cation binding to nucleic acids," Michelle Gill, Scott Strobel, and J.P. Loria J. Am. Chem. Soc. 127, 16723-16732 (2005).
• "Conservation of us-ms enzyme motions in the apo- and substrate mimicked state," Heather Beach, Roger Cole, Michelle Gill, and J.P. Loria J. Am. Chem. Soc. 127, 9167-9176 (2005).
• "Solution structure and dynamics of LuxU from Vibrio harveyi a phosphotransferase protein involved in bacterial quorum sensing," Dagny L. Ulrich, Douglas Kojetin, Bonnie Bassler, John Cavanagh, and J.P. Loria J. Mol. Bio. 347, 297-307 (2005).
• "1H, 15N, and 13C chemical shift assignments of the Vibrio harveyi histidine phosphotransferase protein LuxU," Dagny L. Ulrich, Richele Thompson, Bonnie Bassler, John Cavanagh, and J.P. Loria J. Biomol. NMR 29, 551-552 (2004).
• "Multiple time-scale dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes," Joel A. Butterwick, J.P. Loria, Nathan S. Astrof, Christopher D. Kroenke, Roger Cole, Mark Rance, and Arthur G. Palmer J.Mol. Biol. 339, 855-871 (2004).
• "Off-resonance TROSY (R1rho - R1) for quantitation of fast exchange processes in large proteins," James G. Kempf, Ju-yeon Jung, N.S. Sampson, and J.P. Loria, J. Am. Chem. Soc 125, 12064-5 (2003).
• "Temperature dependence of the backbone dynamics of Ribonuclease A in the ground state and bound to the inhibitor, 5'-phosphothymidine (3'-5')-pyrophosphate adenosine 3'-phosphate," Evgenii Kovrigin, Roger Cole and J.P. Loria, Biochemistry 42, 5279-5291 (2003).
• "FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data," Roger Cole and J.P. Loria, Journal of Biomolecular NMR 26, 203-213 (2003).
• "Protein dynamics from solution NMR: Theory and applications," James G. Kempf and J.P. Loria, Cell Biochemistry & Biophysics 39, 187-212 (2002).
• "Evidence for flexibility in the function of Ribonuclease A," Roger Cole and J.P. Loria, Biochemistry 41, 6072-6081 (2002).
• "NMR methods for quantifying microsecond-millisecond motions in biological macromolecules," A.G. Palmer, C.D. Kroenke, and J.P. Loria, Methods. Enzymol. 339, 204-238 (2001).
• "The static magnetic field dependence of chemical exchange linebroadening defines the NMR chemical shift time scale," O. Millet, J.P. Loria, C.D. Kroenke, M. Pons, and A.G. Palmer, J. Am. Chem. Soc. 122, 2867-2877 (2000).
• "Transverse-relaxation-optimized (TROSY) gradient-enhanced triple-resonance NMR spectroscopy," J.P. Loria, M. Rance, and A.G. Palmer, J. Magn. Reson. 141, 180-184 (1999).
• "A TROSY CPMG sequence for characterizing chemical exchange in large proteins," J.P. Loria, M. Rance, and A.G. Palmer, J. Biomol. NMR. 15. 151-155 (1999).
• "Relaxation-compensated Carr-Purcell-Meiboom-Gill experiments for characterizing kinetic processes by NMR spectroscopy," J.P. Loria, M. Rance, and A.G. Palmer, J. Am. Chem. Soc. 121, 2331-2332 (1999).
• "Sensitivity improvement in transverse relaxation optimized spectroscopy (TROSY)," M. Rance, J.P. Loria, and A.G. Palmer, J. Magn. Reson. 136, 82-102 (1999).
• "Longitudinal and transverse 1H-15N chemical shift anisotropy relaxation interference: Unambiguous determination of rotational diffusion tensors and chemical exchange effects in biological macromolecules," C.D. Kroenke, J.P. Loria, L.K. Lee, M. Rance, and A.G. Palmer, J. Am. Chem. Soc. 120, 7905-7915 (1998).