Evaluating the Intrinsic Cysteine Redox-Dependent States of the A-Chain of Human Insulin Using NMR Spectroscopy, Quantum Chemical Calculations, and Mass Spectrometry
Sharma AK, Ling Y, Greer AB, Hafler DA, Kent SC, Zhang Y, Rigby AC. Evaluating the Intrinsic Cysteine Redox-Dependent States of the A-Chain of Human Insulin Using NMR Spectroscopy, Quantum Chemical Calculations, and Mass Spectrometry. The Journal Of Physical Chemistry B 2009, 114: 585-591. PMID: 19954153, PMCID: PMC2829747, DOI: 10.1021/jp908729h.Peer-Reviewed Original ResearchConceptsQuantum chemical calculationsChemical calculationsFree thiol moietyNMR spectroscopy dataA-chain peptideRedox chemistryNMR spectroscopyThiol moietyCell surface class II moleculesMass spectrometry analysisOxidized stateFunctional studiesA-chain analogueIntrinsic cysteine residuesMass spectrometryPeptide interactionsConformational equilibriumSpectroscopy dataRedox-dependent mechanismDisulfide conformationSpectrometry analysisDependent conformational equilibriumPrevious functional studiesConformationProtein systems