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
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
1992
Dimerization of Glycophorin a Transmembrane Helices: Mutagenesis and Modeling
Engelman D, Adair B, Brünger A, Flanagan J, Lemmon M, Treutlein H, Zhang J. Dimerization of Glycophorin a Transmembrane Helices: Mutagenesis and Modeling. Jerusalem Symposia 1992, 25: 115-125. DOI: 10.1007/978-94-011-2718-9_11.Peer-Reviewed Original ResearchTransmembrane domainSingle transmembrane domainSite-specific mutagenesisGpA dimerTransmembrane helicesDeletion mutagenesisTransmembrane portionCarboxy terminusDimer interfaceHanded supercoilMutagenesisChimera formLipid bilayersGlycophorin AStaphylococcal nucleaseHuman erythrocyte sialoglycoproteinSDS-PAGEErythrocyte sialoglycoproteinDimerizationClose associationDomainDimersSupercoilsNucleaseTerminus
1987
Transmembrane topography of the nicotinic acetylcholine receptor delta subunit.
McCrea P, Popot J, Engelman D. Transmembrane topography of the nicotinic acetylcholine receptor delta subunit. The EMBO Journal 1987, 6: 3619-3626. PMID: 3428268, PMCID: PMC553829, DOI: 10.1002/j.1460-2075.1987.tb02693.x.Peer-Reviewed Original ResearchConceptsDisulfide bridgesAcetylcholine receptor delta subunitIntermolecular disulfide bridgesTransmembrane topographyTransmembrane segmentsTransmembrane crossingReceptor delta subunitCellular locationC-terminusN-terminusDelta subunitNicotinic acetylcholine receptorsSubunitsElectric organVesiclesPermeability barrierTorpedo marmorataVesicle systemAcetylcholine receptorsDiphtheria toxinAqueous spaceDimers