2001
Computation and mutagenesis suggest a right‐handed structure for the synaptobrevin transmembrane dimer
Fleming K, Engelman D. Computation and mutagenesis suggest a right‐handed structure for the synaptobrevin transmembrane dimer. Proteins Structure Function And Bioinformatics 2001, 45: 313-317. PMID: 11746678, DOI: 10.1002/prot.1151.Peer-Reviewed Original ResearchConceptsTransmembrane dimerSingle transmembrane segmentBiological membrane fusionProtein-protein interactionsRight-handed structureInterhelical hydrogen bondsSequence-specific mannerTransmembrane segmentsDimerization motifThree-dimensional structureMutagenesis studiesMembrane fusionSuccessful structure predictionSide-chain atomsStructure predictionSpecific mannerKey playersComputational searchDimersSynaptobrevinMutagenesisComputational methodsAssociation thermodynamicsMotifGlycophorin
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