1999
Multistep Denaturation of Borrelia burgdorferi OspA, a Protein Containing a Single-Layer β-Sheet †
Koide S, Bu Z, Risal D, Pham T, Nakagawa T, Tamura A, Engelman D. Multistep Denaturation of Borrelia burgdorferi OspA, a Protein Containing a Single-Layer β-Sheet †. Biochemistry 1999, 38: 4757-4767. PMID: 10200164, DOI: 10.1021/bi982443+.Peer-Reviewed Original ResearchConceptsSolution small-angle X-ray scatteringChemical shift differencesSingle-layer β-sheetSignificant kinetic barrierSmall-angle X-ray scatteringHeteronuclear NMR spectroscopyDifferential scanning calorimetryNMR spectroscopyRadius of gyrationX-ray scatteringDenaturation reactionNMR measurementsShift differencesKinetic barrierRigid moleculesScanning calorimetrySAXS measurementsΒ-sheetCooperative transitionReactionLys residuesBorrelia burgdorferi OspANative proteinBeta-sheet segmentThermal denaturation reaction
1994
Validation of 13C NMR measurements of liver glycogen in vivo
Gruetter R, Magnusson I, Rothman D, Avison M, Shulman R, Shulman G. Validation of 13C NMR measurements of liver glycogen in vivo. Magnetic Resonance In Medicine 1994, 31: 583-588. PMID: 8057810, DOI: 10.1002/mrm.1910310602.Peer-Reviewed Original Research
1990
Observation by 13C NMR of the EPSP synthase tetrahedral intermediate bound to the enzyme active site.
Anderson K, Sammons R, Leo G, Sikorski J, Benesi A, Johnson K. Observation by 13C NMR of the EPSP synthase tetrahedral intermediate bound to the enzyme active site. Biochemistry 1990, 29: 1460-5. PMID: 2334707, DOI: 10.1021/bi00458a017.Peer-Reviewed Original ResearchConceptsEnzyme active siteTetrahedral intermediateFormation of pyruvateActive siteEnzyme sitesComparison of quenchingReaction of enzymeTime of incubationTetrahedral centerCompound giving riseReaction pathwaysEnzymatic hydrolysisPeak assignmentsEnzymeNMR experimentsTernary complexNMR measurementsSide productsRate of formationSpectroscopic probesLong time of incubationNMRSpeciesTriethylamineCovalent adducts
1974
CO2 Adducts of Certain Amino Acids, Peptides, and Sperm Whale Myoglobin Studied by Carbon 13 and Proton Nuclear Magnetic Resonance
Morrow J, Keim P, Gurd F. CO2 Adducts of Certain Amino Acids, Peptides, and Sperm Whale Myoglobin Studied by Carbon 13 and Proton Nuclear Magnetic Resonance. Journal Of Biological Chemistry 1974, 249: 7484-7494. PMID: 4436319, DOI: 10.1016/s0021-9258(19)81264-4.Peer-Reviewed Original ResearchConceptsNuclear magnetic resonanceAmino acidsProton nuclear magnetic resonanceDeuterium isotope effectChemical shiftsCO2 adductCertain amino acidsSperm whale myoglobinNMR measurementsMagnetic resonanceCarbon-13Fast exchangeMost amino acidsEquilibrium constantsCarbamino adductsIsotope effectWhale myoglobinStructural consequencesAdductsAcidPeptidesAccurate determinationNMRResonanceSensitive function
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