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 thermodynamicsMotifGlycophorinThe Cα—H⋅⋅⋅O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
Senes A, Ubarretxena-Belandia I, Engelman D. The Cα—H⋅⋅⋅O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 9056-9061. PMID: 11481472, PMCID: PMC55372, DOI: 10.1073/pnas.161280798.Peer-Reviewed Original ResearchConceptsMembrane protein structuresMembrane protein foldingTransmembrane helix associationTransmembrane helix interactionsHelix-helix interactionsTransmembrane helicesProtein foldingPacking interfaceHelix associationHelix interactionsProtein structureDeterminants of stabilityCalphaStructural motifsHelixSerineFoldingMotifHydrogen bondsImportant determinantInteractionGlycophorinSpecificityCαDeterminants
1998
Structure-based prediction of the stability of transmembrane helix–helix interactions: The sequence dependence of glycophorin A dimerization
MacKenzie K, Engelman D. Structure-based prediction of the stability of transmembrane helix–helix interactions: The sequence dependence of glycophorin A dimerization. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 3583-3590. PMID: 9520409, PMCID: PMC19879, DOI: 10.1073/pnas.95.7.3583.Peer-Reviewed Original ResearchConceptsHelix-helix interactionsTransmembrane helix-helix associationTransmembrane helix-helix interactionsHelix-helix associationSingle-point mutantsStructure-based predictionTransmembrane domainMembrane proteinsDimer interfaceDimerization propensitySide-chain hydrophobicityDimer stabilityPoint mutationsSteric clashesMultiple mutationsMutationsSequence dependenceCompensatory effectFavorable van der Waals interactionsMutantsFoldingProteinInteractionDimerizationGlycophorin