1988
Phosphorylation of ankyrin down‐regulates its cooperative interaction with spectrin and protein 3
Cianci C, Giorgi M, Morrow J. Phosphorylation of ankyrin down‐regulates its cooperative interaction with spectrin and protein 3. Journal Of Cellular Biochemistry 1988, 37: 301-315. PMID: 2970468, DOI: 10.1002/jcb.240370305.Peer-Reviewed Original ResearchConceptsCytoplasmic domainAffinity of ankyrinProtein 3Integral membrane proteinsSpectrin tetramersCooperative interactionsSpectrin oligomersMembrane kinaseSpectrin dimersLong-range cooperative interactionsNonerythroid cellsProtein phosphorylationMembrane proteinsPeripheral cytoskeletonBeta spectrinAnkyrinPhosphorylationOligomer formationChymotryptic digestionSpectrinPrimary attachmentGeneral importanceCooperative fashionEnhanced affinitySuch interactions
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 nuclei
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 acid