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-dodecyl
1997
The effect of point mutations on the free energy of transmembrane α-helix dimerization11Edited by M. F. Moody
Fleming K, Ackerman A, Engelman D. The effect of point mutations on the free energy of transmembrane α-helix dimerization11Edited by M. F. Moody. Journal Of Molecular Biology 1997, 272: 266-275. PMID: 9299353, DOI: 10.1006/jmbi.1997.1236.Peer-Reviewed Original ResearchConceptsSodium dodecylsulfateVan der Waals interactionsAnalytical ultracentrifugationDer Waals interactionsFree energyMolecular association eventsEnergy of dimerizationOctyl etherWaals interactionsMolecular modelingRelative energy scaleDetergent environmentReversible associationEnergy differenceSedimentation equilibriumMonomersTransmembrane α-helicesNon-denaturing detergent solutionsDimer formationΑ-helixDimer stateAssociation eventsDetergent solutionDissociationHelixA Transmembrane Helix Dimer: Structure and Implications
MacKenzie K, Prestegard J, Engelman D. A Transmembrane Helix Dimer: Structure and Implications. Science 1997, 276: 131-133. PMID: 9082985, DOI: 10.1126/science.276.5309.131.Peer-Reviewed Original ResearchConceptsMembrane-spanning alpha helicesSolution nuclear magnetic resonance spectroscopyDimeric transmembrane domainNuclear magnetic resonance spectroscopyTransmembrane helix dimerVan der Waals interactionsDer Waals interactionsAqueous detergent micellesIntermonomer hydrogen bondsTransmembrane helicesTransmembrane domainMagnetic resonance spectroscopyThree-dimensional structureDetergent micellesHelix dimerHydrogen bondsWaals interactionsAlpha-helixResonance spectroscopyGlycophorin ASpecific associationHelixSequence dependenceMicellesSpectroscopy
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