2001
The 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 determinantInteractionGlycophorinSpecificityCαDeterminantsPolar residues drive association of polyleucine transmembrane helices
Zhou F, Merianos H, Brunger A, Engelman D. Polar residues drive association of polyleucine transmembrane helices. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 2250-2255. PMID: 11226225, PMCID: PMC30124, DOI: 10.1073/pnas.041593698.Peer-Reviewed Original ResearchConceptsPolar residuesPolyleucine sequenceHelix associationTransmembrane helix associationInterhelical hydrogen bondingTransmembrane protein functionTransmembrane helicesForm homoProtein functionTransmembrane proteinDrive associationMembrane proteinsDetergent micellesAsparagine residuesGeneral structural featuresBiological membranesResiduesOligomerization specificityProteinSequenceHelixStructural flexibilitySuch interactionsStructural featuresHeterooligomers
2000
Interhelical hydrogen bonding drives strong interactions in membrane proteins
Xiao Zhou F, Cocco M, Russ W, Brunger A, Engelman D. Interhelical hydrogen bonding drives strong interactions in membrane proteins. Nature Structural & Molecular Biology 2000, 7: 154-160. PMID: 10655619, DOI: 10.1038/72430.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAsparagineCell MembraneChloramphenicol O-AcetyltransferaseCircular DichroismDetergentsDimerizationDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelFungal ProteinsGlycophorinsHydrogen BondingLeucine ZippersMagnetic Resonance SpectroscopyMembrane ProteinsMicellesMicrococcal NucleaseMolecular Sequence DataPeptidesProtein ConformationProtein KinasesProtein Structure, SecondaryRecombinant ProteinsSaccharomyces cerevisiae ProteinsConceptsMembrane proteinsHelix associationTransmembrane α-helicesIntegral membrane proteinsInterhelical hydrogen bondingModel transmembrane helixTransmembrane helicesMembrane helicesGCN4 leucine zipperLeucine zipperPolar residuesSoluble proteinHydrophobic leucineΑ-helixBiological membranesProteinHelixNon-specific interactionsValine (HAV) sequenceMembraneZipperFoldingMotifAsparagineResidues
1999
Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain 11Edited by G. von Heijne
Fisher L, Engelman D, Sturgis J. Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain 11Edited by G. von Heijne. Journal Of Molecular Biology 1999, 293: 639-651. PMID: 10543956, DOI: 10.1006/jmbi.1999.3126.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceButyratesCircular DichroismDetergentsDimerizationEnergy TransferFluorescent DyesGlycophorinsHumansKineticsMicellesMolecular Sequence DataPeptide FragmentsPhosphorylcholineProtein Structure, SecondaryQuaternary Ammonium CompoundsSodium Dodecyl SulfateSolventsSpectrometry, FluorescenceThermodynamicsConceptsSpecific chemical interactionsFörster resonance energy transferResonance energy transferSodium dodecyl sulfateComplex solventChemical interactionFar-UV circular dichroismCircular dichroismDodecyl sulfateTransmembrane helix associationDetergent micellesHelix associationEnergy transferThermodynamic measurementsHelix formationObserved KdZwitterionic detergentSecondary structureDimerizationG. von HeijneHelix dimerizationOrders of magnitudeDetergentsTransmembrane helicesTransmembrane domainA Method for Determining Transmembrane Helix Association and Orientation in Detergent Micelles Using Small Angle X-Ray Scattering
Bu Z, Engelman D. A Method for Determining Transmembrane Helix Association and Orientation in Detergent Micelles Using Small Angle X-Ray Scattering. Biophysical Journal 1999, 77: 1064-1073. PMID: 10423450, PMCID: PMC1300396, DOI: 10.1016/s0006-3495(99)76956-0.Peer-Reviewed Original ResearchMeSH KeywordsBiophysical PhenomenaBiophysicsButyratesDetergentsDimerizationElectrochemistryGlycophorinsHumansIn Vitro TechniquesMembrane ProteinsMicellesMolecular WeightMutationProtein ConformationProtein Structure, SecondaryQuaternary Ammonium CompoundsRecombinant Fusion ProteinsScattering, RadiationSolutionsSolventsX-RaysConceptsDetergent micellesTransmembrane domainAlpha-helical transmembrane domainsSolution small-angle X-ray scatteringTransmembrane helix associationSolution small-angle X-rayHuman erythrocyte glycophorin ASmall-angle X-ray scatteringMembrane proteinsTransmembrane proteinErythrocyte glycophorin ACarboxyl terminusHelix associationAngle X-ray scatteringGlycophorin AStaphylococcal nucleaseSmall-angle X-rayProteinModel systemMicelle contributionX-ray scatteringAngle X-rayDimerizationGyration analysisN-dodecylTOXCAT: A measure of transmembrane helix association in a biological membrane
Russ W, Engelman D. TOXCAT: A measure of transmembrane helix association in a biological membrane. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 863-868. PMID: 9927659, PMCID: PMC15316, DOI: 10.1073/pnas.96.3.863.Peer-Reviewed Original ResearchMeSH KeywordsATP-Binding Cassette TransportersBacterial ProteinsBase SequenceCarrier ProteinsCell MembraneChloramphenicol O-AcetyltransferaseDNA PrimersDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGene LibraryGenes, ReporterGenetic Complementation TestMacromolecular SubstancesMaltose-Binding ProteinsMembrane ProteinsModels, MolecularMolecular Sequence DataMonosaccharide Transport ProteinsPeriplasmic Binding ProteinsProtein FoldingProtein Structure, SecondaryRecombinant Fusion ProteinsSpheroplastsTranscription FactorsConceptsTOXCAT systemDetergent micellesHelical membrane proteinsN-terminal DNATransmembrane helix associationTransmembrane alpha-helixReporter gene encoding chloramphenicolNatural membrane environmentGene encoding chloramphenicolTransmembrane domainTM associationTM dimerizationMembrane proteinsMembrane environmentOligomerization motifPolar residuesAlpha-helixHelix associationSequence specificityChimeric constructsCAT expressionBiological membranesFundamental eventNoncovalent associationAssay distinguishes
1994
Specificity and promiscuity in membrane helix interactions
Lemmon M, Engelman D. Specificity and promiscuity in membrane helix interactions. Quarterly Reviews Of Biophysics 1994, 27: 157-218. PMID: 7984776, DOI: 10.1017/s0033583500004522.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsTransmembrane α-helicesMembrane proteinsΑ-helixMembrane protein foldingMembrane-spanning portionTransmembrane helix associationHelix-helix interactionsParticular helicesProtein foldingHelix associationHelix interactionsProsthetic groupLipid bilayersCharge-charge interactionsStereochemical fitFoldingProteinAccessible statesSpecificityOligomerizationInteractionPromiscuityHelixAssemblyA dimerization motif for transmembrane α–helices
Lemmon M, Treutlein H, Adams P, Brünger A, Engelman D. A dimerization motif for transmembrane α–helices. Nature Structural & Molecular Biology 1994, 1: 157-163. PMID: 7656033, DOI: 10.1038/nsb0394-157.Peer-Reviewed Original ResearchConceptsTransmembrane α-helicesHydrophobic transmembrane α-helicesSpecific helix-helix interactionsΑ-helixIntegral membrane proteinsHelix-helix interactionsHelix-helix interfaceDimerization motifSpecific dimerizationMembrane proteinsHelix associationFunctional analysisAmino acidsSuch motifsLipid bilayersMotifParticular motifsFoldingDimerizationSuch interactionsComplex membranesProteinOligomerizationVariety of systemsInteraction