1976
Carbon 13 resonances of 13CO2 carbamino adducts of alpha and beta chains in human adult hemoglobin.
Morrow J, Matthew J, Wittebort R, Gurd F. Carbon 13 resonances of 13CO2 carbamino adducts of alpha and beta chains in human adult hemoglobin. Journal Of Biological Chemistry 1976, 251: 477-484. PMID: 1395, DOI: 10.1016/s0021-9258(17)33904-2.Peer-Reviewed Original Research
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 functionCarbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Methionine, Proline, Arginine, and Lysine
Keim P, Vigna R, Nigen A, Morrow J, Gurd F. Carbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Methionine, Proline, Arginine, and Lysine. Journal Of Biological Chemistry 1974, 249: 4149-4156. PMID: 4850872, DOI: 10.1016/s0021-9258(19)42496-4.Peer-Reviewed Original ResearchConceptsChemical shiftsCarbon-13 nuclear magnetic resonanceLysine peptidesPyrrolidine ringNuclear magnetic resonance spectroscopyState of protonationChemical shift assignmentsNuclear magnetic resonanceSide chain groupsCentral residuesMagnetic resonance spectroscopyAdjacent glycine residuesΕ-amino groupSpin-lattice relaxation timePeptide backboneShift assignmentsChain groupsRatio of transConformational flexibilitySide chainsTrans formResonance spectroscopyNatural abundancePK valuesCarbon nuclei13C NMR Studies of the Interaction of Hb and Carbonic Anhydrase with 13CO2
Gurd F, Morrow J, Keim P, Visscher R, Marshall R. 13C NMR Studies of the Interaction of Hb and Carbonic Anhydrase with 13CO2. Advances In Experimental Medicine And Biology 1974, 48: 109-124. PMID: 4215298, DOI: 10.1007/978-1-4684-0943-7_6.Peer-Reviewed Original ResearchConceptsMetal-protein interactionsInteraction of CO2NMR studiesHydrated derivativeNMR spectrometerSmall moleculesInteraction of HbCarbonate saltsBuffer componentsBicarbonate ionsCarbonic anhydraseCO2NMRUnquestionable importanceCommon strategySpeciesProteinIonsInsolubilityMoleculesSaltInteractionDerivativesBicarbonateSpectrometer
1973
Carbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Serine, Threonine, Aspartic and Glutamic Acids, Asparagine, and Glutamine
Keim P, Vigna R, Morrow J, Marshall R, Gurd F. Carbon 13 Nuclear Magnetic Resonance of Pentapeptides of Glycine Containing Central Residues of Serine, Threonine, Aspartic and Glutamic Acids, Asparagine, and Glutamine. Journal Of Biological Chemistry 1973, 248: 7811-7818. PMID: 4750428, DOI: 10.1016/s0021-9258(19)43261-4.Peer-Reviewed Original ResearchConceptsChemical shiftsGroup protonationCarbon-13 nuclear magnetic resonanceNuclear magnetic resonance spectroscopyState of protonationSide chain groupsNuclear magnetic resonanceNatural abundance 13CAmino group protonationPK valuesCentral residuesMagnetic resonance spectroscopySpin-lattice relaxation timeAspartic acid (RGD) peptideGlutamic acid peptideΒ-carbonChain groupsResonance spectroscopyProtonationSensitive resonancePH dependenceDissociation constantsEffect of aggregationCarbon nucleiGlutamic acidInteraction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations
Morrow J, Keim P, Visscher R, Marshall R, Gurd F. Interaction of 13CO2 and Bicarbonate with Human Hemoglobin Preparations. Proceedings Of The National Academy Of Sciences Of The United States Of America 1973, 70: 1414-1418. PMID: 4514311, PMCID: PMC433509, DOI: 10.1073/pnas.70.5.1414.Peer-Reviewed Original ResearchCarbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins Carboxymethylated with Enriched [2-13C]Bromoacetate
Nigen A, Keim P, Marshall R, Morrow J, Vigna R, Gurd F. Carbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins Carboxymethylated with Enriched [2-13C]Bromoacetate. Journal Of Biological Chemistry 1973, 248: 3724-3732. PMID: 4735715, DOI: 10.1016/s0021-9258(19)43986-0.Peer-Reviewed Original Research
1972
Carbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins and Ribonuclease A Carboxymethylated with Enriched [2-13C]Bromoacetate
Nigen A, Keim P, Marshall R, Morrow J, Gurd F. Carbon 13 Nuclear Magnetic Resonance Spectroscopy of Myoglobins and Ribonuclease A Carboxymethylated with Enriched [2-13C]Bromoacetate. Journal Of Biological Chemistry 1972, 247: 4100-4102. PMID: 5033404, DOI: 10.1016/s0021-9258(19)45145-4.Peer-Reviewed Original ResearchConceptsCarbon-13 nuclear magnetic resonance spectroscopyNuclear magnetic resonance spectroscopyNuclear magnetic resonanceΑ-carbon atomNuclear magnetic resonance signalsMagnetic resonance spectroscopyEnriched adductsChemical shiftsBovine pancreatic ribonuclease APancreatic ribonuclease AResonance spectroscopyCarbon atomsDetermination of T1Resonance signalsRibonuclease AMagnetic resonance signalDetailed interpretationMagnetic resonanceSmall proteinsResonanceSpectroscopyDeterminationAdductsAtomsCarboxymethylated