2003
Amphipols: polymeric surfactants for membrane biology research
Popot J, Berry E, Charvolin D, Creuzenet C, Ebel C, Engelman D, Flötenmeyer M, Giusti F, Gohon Y, Hervé P, Hong Q, Lakey J, Leonard K, Shuman H, Timmins P, Warschawski D, Zito F, Zoonens M, Pucci B, Tribet C. Amphipols: polymeric surfactants for membrane biology research. Cellular And Molecular Life Sciences 2003, 60: 1559-1574. PMID: 14513831, PMCID: PMC11138540, DOI: 10.1007/s00018-003-3169-6.Peer-Reviewed Original ResearchConceptsMembrane proteinsQuasi-irreversible mannerPolymeric surfactantsAmphiphilic polymersMembrane biologyAqueous solutionTransmembrane surfaceAmphipolsBiology researchDissociating characterPutative usesNative stateSurfactantsNovel familyProteinCurrent knowledgeRapid inactivationNoncovalentDetergentsPolymersBiologyCompoundsComplexesInactivationAbsence
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 solutionDissociationHelix
1995
Small angle x-ray scattering studies of magnetically oriented lipid bilayers
Hare B, Prestegard J, Engelman D. Small angle x-ray scattering studies of magnetically oriented lipid bilayers. Biophysical Journal 1995, 69: 1891-1896. PMID: 8580332, PMCID: PMC1236422, DOI: 10.1016/s0006-3495(95)80059-7.Peer-Reviewed Original ResearchConceptsNuclear magnetic resonanceLipid bilayersMembrane-associated moleculesBilayer thicknessLipid particlesSmall-angle X-rayX-ray scatteringAngle X-rayNMR dataDLPC vesiclesOrientational parametersX-ray solutionMolar ratioPhospholipid moleculesStructural studiesOrientational energyPhospholipid bilayersAnalogue 3MoleculesBilayersInterparticle spacingX-rayMagnetic resonanceParticlesComplexes
1971
Structural comparisons of native and reaggregated membranes from Mycoplasma laidlawii and erythrocytes by X-ray diffraction and nuclear magnetic resonance techniques
Metcalfe J, Metcalfe S, Engelman D. Structural comparisons of native and reaggregated membranes from Mycoplasma laidlawii and erythrocytes by X-ray diffraction and nuclear magnetic resonance techniques. Biochimica Et Biophysica Acta 1971, 241: 412-421. PMID: 5159791, DOI: 10.1016/0005-2736(71)90041-1.Peer-Reviewed Original ResearchMeSH KeywordsAcetoneAcholeplasma laidlawiiAlcoholsBacterial ProteinsBenzyl CompoundsBinding SitesCell MembraneCentrifugation, Density GradientChemical PrecipitationDetergentsDeuteriumDialysisErythrocytesLipidsMacromolecular SubstancesMagnetic Resonance SpectroscopyMicroscopy, ElectronMycoplasmaSulfatesUltracentrifugationX-Ray DiffractionConceptsRelaxation measurementsMagnetic relaxation measurementsNuclear magnetic relaxation measurementsNuclear magnetic resonance techniquesNative membranesProbe experimentsX-ray diffraction patternsX-ray diffractionMagnetic resonance techniquesSodium dodecyl sulfateLipid bilayer structureProbe techniqueProbe moleculesBenzyl alcoholResonance techniquesDiffraction patternsBilayer regionsDodecyl sulfateBilayer structureElectron microscopyMembrane systemStructural comparisonMeasurementsMembraneDiffractionStructural comparisons of native and reaggregated membranes from Mycoplasma laidlawii and erythrocytes using a fluorescence probe
Metcalfe S, Metcalfe J, Engelman D. Structural comparisons of native and reaggregated membranes from Mycoplasma laidlawii and erythrocytes using a fluorescence probe. Biochimica Et Biophysica Acta 1971, 241: 422-430. PMID: 5159792, DOI: 10.1016/0005-2736(71)90042-3.Peer-Reviewed Original Research
1967
Characterization of the plasma membrane of Mycoplasma laidlawii. I. Sodium dodecyl sulfate solubilization
Engelman D, Terry T, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. I. Sodium dodecyl sulfate solubilization. Biochimica Et Biophysica Acta 1967, 135: 381-390. PMID: 6048810, DOI: 10.1016/0005-2736(67)90028-4.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfate solubilizationProtein-detergent complexesSeparate lipidsDetergent solubilizationAnalytical ultracentrifugationPlasma membraneLipoprotein subunitsSchlieren peakSchlieren patternsSolubilizationDistribution of proteinsPreparationSolubilized membrane preparationsMembrane proteinsMembraneIntermediatesMycoplasma laidlawiiDensity gradient sedimentationComplexesMembrane preparationsProteinCharacterizationLipidsPropertiesUltracentrifugationCharacterization of the plasma membrane of Mycoplasma laidlawii. II. Modes of aggregation of solubilized membrane components
Terry T, Engelman D, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. II. Modes of aggregation of solubilized membrane components. Biochimica Et Biophysica Acta 1967, 135: 391-405. PMID: 6058126, DOI: 10.1016/0005-2736(67)90029-6.Peer-Reviewed Original Research