2024
Kinetic study of membrane protein interactions: from three to two dimensions
Adrien V, Reffay M, Taulier N, Verchère A, Monlezun L, Picard M, Ducruix A, Broutin I, Pincet F, Urbach W. Kinetic study of membrane protein interactions: from three to two dimensions. Scientific Reports 2024, 14: 882. PMID: 38195620, PMCID: PMC10776792, DOI: 10.1038/s41598-023-50827-5.Peer-Reviewed Original ResearchConceptsMembrane proteinsMembrane protein interactionsProtein-protein interactionsProtein complexesProtein interactionsMembrane environmentOpposite membranesBacterial efflux pumpsProtein behaviorProtein systemsMolecular interactionsEfflux pumpsProteinExploration distanceMembraneFluorescence recovery experimentsInteractionBinding rateBinding constantsComplexes
2009
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
2002
Energy of Hydrogen Bonds Probed by the Adhesion of Functionalized Lipid Layers
Tareste D, Pincet F, Perez E, Rickling S, Mioskowski C, Lebeau L. Energy of Hydrogen Bonds Probed by the Adhesion of Functionalized Lipid Layers. Biophysical Journal 2002, 83: 3675-3681. PMID: 12496134, PMCID: PMC1302442, DOI: 10.1016/s0006-3495(02)75367-8.Peer-Reviewed Original ResearchConceptsHydrogen bondsIntramolecular hydrogen bondsHydrogen-bonding groupsSurface force apparatusSingle hydrogen bondHydrogen-bonding partsMonolayer of lipidsDifferent energetic contributionsForce apparatusHydrophobic interactionsInteraction energyBondsKcal/Lipid layerEnergetic contributionsTheoretical studyAdhesion energyProtein systemsBond partProtein foldingProtein stabilizationHeadgroupsWaterSurfaceComplex structure
1996
Leucine side-chain rotamers in a glycophorin A transmembrane peptide as revealed by three-bond carbon—carbon couplings and 13C chemical shifts
MacKenzie K, Prestegard J, Engelman D. Leucine side-chain rotamers in a glycophorin A transmembrane peptide as revealed by three-bond carbon—carbon couplings and 13C chemical shifts. Journal Of Biomolecular NMR 1996, 7: 256-260. PMID: 8785502, DOI: 10.1007/bf00202043.Peer-Reviewed Original ResearchConceptsChemical shiftsPeptide dimersΑ-carbonSide chainsSide-chain rotamer populationsCarbon-carbon couplingLeucine side chainsThree-bond J couplingsNMR pulse sequencesΔ-methyl groupsRotamer populationsMethyl carbonFast exchangeSide-chain rotamersJ-couplingsTransmembrane peptidesDimer interfaceRotameric statesProtein systemsRotamersShift distributionGlycophorin A.DimersChainMethyl
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