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
Mapping the lipid-exposed surfaces of membrane proteins
Arkin I, MacKenzie K, Fisher L, Aimoto S, Engelman D, Smith S. Mapping the lipid-exposed surfaces of membrane proteins. Nature Structural & Molecular Biology 1996, 3: 240-243. PMID: 8605625, DOI: 10.1038/nsb0396-240.Peer-Reviewed Original ResearchConceptsMembrane proteinsLong transmembrane helixLipid-exposed surfaceThree-dimensional foldHigh-resolution structuresRelative rotational orientationTransmembrane helicesTransmembrane segmentsThird cysteineCysteine residuesLipid environmentHelix interfacePentameric complexProteinLipid interfaceStable complexesHelixResiduesUndergoes exchangeSulphydryl groupsPhospholambanComplexesInternal faceCysteineRotational orientationCoassembly of Synthetic Segments of Shaker K+ Channel within Phospholipid Membranes †
Peled-Zehavi H, Arkin I, Engelman D, Shai Y. Coassembly of Synthetic Segments of Shaker K+ Channel within Phospholipid Membranes †. Biochemistry 1996, 35: 6828-6838. PMID: 8639634, DOI: 10.1021/bi952988t.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsOligomerization of proteinsMembrane-embedded segmentsMembrane-mimetic environmentsAlpha-helical contentAlpha-helical structureLipid/peptide molar ratioS4 regionShaker potassium channelSecondary structure studiesResonance energy transfer measurementsPhospholipid membranesZwitterionic phospholipid vesiclesTransmembrane segmentsMembrane proteinsPhospholipid milieuMimetic environmentsSynthetic segmentsFirst repeatS4 sequenceEel sodium channelS4 segmentEnergy transfer measurementsSecondary structure
1990
Membrane protein folding and oligomerization: the two-stage model.
Popot J, Engelman D. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 1990, 29: 4031-7. PMID: 1694455, DOI: 10.1021/bi00469a001.Peer-Reviewed Original ResearchConceptsMembrane protein foldingIntegral membrane proteinsMembrane proteinsProtein foldingMembrane protein subunitsTransmembrane segmentsTransmembrane structureSequence dataProtein subunitsVariety of functionsAqueous channelsLipid bilayersFoldingProteinSubunitsOligomerizationAssemblyFragmentsBilayers
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
1986
Localization of two chymotryptic fragments in the structure of renatured bacteriorhodopsin by neutron diffraction.
Trewhella J, Popot J, Zaccaï G, Engelman D. Localization of two chymotryptic fragments in the structure of renatured bacteriorhodopsin by neutron diffraction. The EMBO Journal 1986, 5: 3045-3049. PMID: 3792306, PMCID: PMC1167259, DOI: 10.1002/j.1460-2075.1986.tb04604.x.Peer-Reviewed Original Research