2009
Contribution of individual histidines to the global stability of human prolactin
Keeler C, Tettamanzi MC, Meshack S, Hodsdon ME. Contribution of individual histidines to the global stability of human prolactin. Protein Science 2009, 18: 909-920. PMID: 19384991, PMCID: PMC2771294, DOI: 10.1002/pro.100.Peer-Reviewed Original ResearchConceptsIndividual histidineClosest evolutionary cousinsEvolutionary roleDouble mutant cyclesHomologous residuesEvolutionary cousinsNearby histidineExtracellular domainNative proteinTertiary structureStability of hGHNative stateMutant cyclesHuman growth hormoneHistidineStructural interactionsHuman prolactinResiduesPolypeptide hormonesPhysiologic pH rangeFunctional propertiesStructural locationAffinityProteinMutations
2008
Analysis of Site-Specific Histidine Protonation in Human Prolactin ,
Tettamanzi MC, Keeler C, Meshack S, Hodsdon ME. Analysis of Site-Specific Histidine Protonation in Human Prolactin ,. Biochemistry 2008, 47: 8638-8647. PMID: 18652486, PMCID: PMC2766358, DOI: 10.1021/bi800444t.Peer-Reviewed Original ResearchConceptsPH-dependent regulationSite-directed mutagenesisExtracellular domainHistidine residuesHistidine protonationStatistical supportHPRL receptorFunctional propertiesHuman prolactinProtein surfaceBiophysical mechanismsBiophysical originApparent midpointEquilibrium dissociation constantsHistidineResiduesProtein hormonesDetailed understandingCooperativity constantsSurprising numberDissociation rateMutagenesisDissociation constantsProteinNMR spectroscopy
1982
The nature of CuA in cytochrome c oxidase.
Stevens T, Martin C, Wang H, Brudvig G, Scholes C, Chan S. The nature of CuA in cytochrome c oxidase. Journal Of Biological Chemistry 1982, 257: 12106-12113. PMID: 6288707, DOI: 10.1016/s0021-9258(18)33685-8.Peer-Reviewed Original ResearchConceptsCytochrome c oxidaseYeast cytochrome c oxidaseC oxidaseCysteine sulfurProteinBeef heartOxidaseElectron nuclear double resonance (ENDOR) spectraElectron paramagnetic resonanceSubstantial spin densityParamagnetic resonanceDouble resonance spectraBetaCuAResonance spectraCysteineSpin densityHistidine
1968
Identification of the A protein as a structural component of bacteriophage R17
Steitz J. Identification of the A protein as a structural component of bacteriophage R17. Journal Of Molecular Biology 1968, 33: 923-936. PMID: 4178187, DOI: 10.1016/0022-2836(68)90328-8.Peer-Reviewed Original ResearchConceptsA proteinBacteriophage R17Amber mutantsMolecule of histidineProtein monomersProtein productsMajor polypeptidesMolecular weight estimatesStructural componentsPhage particlesR17Non-permissive hostsDefective particlesVirus particlesProteinGel filtrationHistidineCistronMutantsSpheroplastsPolypeptideHostCopiesIsolation of the A protein from bacteriophage R17
Steitz J. Isolation of the A protein from bacteriophage R17. Journal Of Molecular Biology 1968, 33: 937-945. PMID: 5700426, DOI: 10.1016/0022-2836(68)90329-x.Peer-Reviewed Original Research
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