1986
Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin
Harris A, Anderson J, Yurchenco P, Green L, Ainger K, Morrow J. Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin. Journal Of Cellular Biochemistry 1986, 30: 51-69. PMID: 2420811, DOI: 10.1002/jcb.240300107.Peer-Reviewed Original Research
1975
Nuclear Magnetic Resonance Studies Of Hemoglobin: Functional State Correlations And Isotopic Enrichment Strategie
Morrow J, Gurd F, Ho C. Nuclear Magnetic Resonance Studies Of Hemoglobin: Functional State Correlations And Isotopic Enrichment Strategie. Critical Reviews In Biochemistry 1975, 3: 221-287. PMID: 3388, DOI: 10.3109/10409237509105453.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAnimalsBinding SitesCarboxyhemoglobinHemeHemoglobinsHemoglobins, AbnormalHorsesHumansHydrogen-Ion ConcentrationIronMagnetic Resonance SpectroscopyMethemoglobinModels, MolecularMyoglobinOxyhemoglobinsProtein BindingProtein ConformationSpecies SpecificityWhales
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 functionLigand-dependent aggregation of chicken hemoglobin AI
Morrow J, Wittebort R, Gurd F. Ligand-dependent aggregation of chicken hemoglobin AI. Biochemical And Biophysical Research Communications 1974, 60: 1058-1065. PMID: 4429560, DOI: 10.1016/0006-291x(74)90420-3.Peer-Reviewed Original Research13C 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