1997
Structure of the Transmembrane Cysteine Residues in Phospholamban
Arkin I, Adams P, Brünger A, Aimoto S, Engelman D, Smith S. Structure of the Transmembrane Cysteine Residues in Phospholamban. The Journal Of Membrane Biology 1997, 155: 199-206. PMID: 9050443, DOI: 10.1007/s002329900172.Peer-Reviewed Original ResearchConceptsTransmembrane domainCysteine residuesSide chainsPentameric complexCysteine side chainsTransmembrane cysteine residuesLong α-helixIntrahelical hydrogen bondsBackbone carbonyl oxygenSelective ion channelsPolar side chainsElectrostatic potential fieldCarbonyl oxygenSulfhydryl groupsHydrogen bondsMembrane proteinsWild-type phospholambanVibrational spectraMutagenesis studiesTransmembrane peptidesAlanine substitutionsMolecular dynamicsReticulum membraneElectrostatic calculationsΑ-helix
1996
Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban
Ludlam C, Arkin I, Liu X, Rothman M, Rath P, Aimoto S, Smith S, Engelman D, Rothschild K. Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban. Biophysical Journal 1996, 70: 1728-1736. PMID: 8785331, PMCID: PMC1225141, DOI: 10.1016/s0006-3495(96)79735-7.Peer-Reviewed Original ResearchConceptsSite-directed isotope labelingLocal secondary structureIsotope labelingSecondary structureSelective ion channelsTotal reflection Fourier transformPeptide amide groupsAmide IReflection Fourier transformDeuterium/hydrogen exchangeTransmembrane domainMembrane domainsMembrane proteinsTransmembrane orientationAmino acid fragmentSpectroscopic characterizationIon channelsHydrophobic regionAmide carbonylProtein backboneCardiac muscle cellsAmide groupLipid bilayersATPase activityFourier transform