J Patrick Loria, PhD
Professor of Chemistry and of Molecular Biophysics and BiochemistryCards
Appointments
Chemistry
Primary
Contact Info
About
Titles
Professor of Chemistry and of Molecular Biophysics and Biochemistry
Appointments
Chemistry
ProfessorPrimaryMolecular Biophysics and Biochemistry
ProfessorSecondary
Other Departments & Organizations
- Biochemistry, Quantitative Biology, Biophysics and Structural Biology (BQBS)
- Chemistry
- Molecular Biophysics and Biochemistry
- Structural Biology
- Yale Combined Program in the Biological and Biomedical Sciences (BBS)
Education & Training
- NIH Postdoctoral Fellow
- Columbia University (2000)
- PhD
- University of Notre Dame, Biochemistry (1996)
- BS
- George Washington University, Chemistry (1990)
Research
Overview
Medical Research Interests
Biochemistry; Biophysics; Chemistry; Magnetic Resonance Spectroscopy; Molecular Biology; Protein Folding
Research at a Glance
Yale Co-Authors
Frequent collaborators of J Patrick Loria's published research.
Research Interests
Research topics J Patrick Loria is interested in exploring.
Victor Batista
Magnetic Resonance Spectroscopy
Publications
2024
A salt bridge of the C‐terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity
Zavala E, Dansereau S, Burke M, Lipchock J, Maschietto F, Batista V, Loria J. A salt bridge of the C‐terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity. Protein Science 2024, 33: e5009. PMID: 38747379, PMCID: PMC11094782, DOI: 10.1002/pro.5009.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsConceptsCatalytic activityPhenylphosphonic acidAnalysis of molecular dynamics trajectoriesNMR chemical shiftsSalt bridgesMolecular dynamics trajectoriesC-terminal carboxyl groupChemical shiftsCombination of solution NMRMolecular dynamicsGuanidinium moietyCarboxyl groupsPara-nitrophenylphosphateSolution NMRActive site inhibitorsHistidine phosphataseActive siteElectrostatic interactionsDynamics trajectoriesEnzymatic functionC-terminusGlycine residuesSubstrate affinityBiochemical experimentsBinding affinity
2009
Role of Loop−Loop Interactions in Coordinating Motions and Enzymatic Function in Triosephosphate Isomerase
Wang Y, Berlow RB, Loria JP. Role of Loop−Loop Interactions in Coordinating Motions and Enzymatic Function in Triosephosphate Isomerase. Biochemistry 2009, 48: 4548-4556. PMID: 19348462, PMCID: PMC2713366, DOI: 10.1021/bi9002887.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsLoop 7Triosephosphate isomeraseLoop 6Chicken triosephosphate isomeraseC-terminal hingeActive site loopActive site loop motionArchaeal homologueEnzyme triosephosphate isomeraseMutant enzymesEnzymatic functionProtein sequencesBiological functionsSite loopEnzymatic activityFold lossTemperature-dependent NMR experimentsLoop motionModel systemIsomeraseSequenceActive siteEnzymeEnzymatic reactionsMutants
2007
The mechanism of rate-limiting motions in enzyme function
Watt ED, Shimada H, Kovrigin EL, Loria JP. The mechanism of rate-limiting motions in enzyme function. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 11981-11986. PMID: 17615241, PMCID: PMC1924554, DOI: 10.1073/pnas.0702551104.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsEnzyme functionProtein motionsCluster of residuesRate-limiting enzymatic stepEnzyme active siteActive siteNMR relaxation experimentsSingle residueEnzymatic stepsConformational flexibilityRate-limiting stepKey modulatorHistidine-48RNaseResiduesSingle siteMutantsSitesMutationsEnzymeH48Solvent isotope effectFunctionHallmarkExchangeable protons
Academic Achievements & Community Involvement
honor Camille and Henry Dreyfus New Faculty Fellow
National AwardDetails01/01/2001United Stateshonor Alfred P. Sloan Fellowship
International AwardDetailsUnited States