2021
Cell Boundaries, How Membranes and Their Proteins Work
White S, von Heijne G, Engelman D. Cell Boundaries, How Membranes and Their Proteins Work. 2021 DOI: 10.1201/9780429341328.Peer-Reviewed Original ResearchHigh-resolution micrographsMembrane proteinsMolecular mechanismsOrganization of lipidsBasic physicsWide arrayCell membranePhysicsProteinCentral discoveryBiologyPhysics studentsMembraneBiophysical foundationConcerted useCell boundariesDiscoveryPhysical chemistryAdvanced undergraduateDiagramArrayFoldingOrganizational principlesStructureMicrographs
2009
Translocating cell‐impermeable molecules through the plasma membrane of cancer cells
THEVENIN D, An M, Andreev O, Reshetnyak Y, Engelman D. Translocating cell‐impermeable molecules through the plasma membrane of cancer cells. The FASEB Journal 2009, 23: 796.7-796.7. DOI: 10.1096/fasebj.23.1_supplement.796.7.Peer-Reviewed Original ResearchCell-impermeable moleculesCell-impermeable cargo moleculesDrug designLipid bilayersHost-guest modelMembrane-impermeable cargoNovel delivery systemPhysiological pHTraverse membranesModel cargoCancer cell membraneDelivery systemCargo moleculesMoleculesCargo propertiesBilayersPeptidesMembraneSingle amino acidPropertiesC-terminusAmino acidsPotential therapeutic agentTherapeutic agentsAcidity
2006
Isolation and Identification of Membrane Protein Oligomers from the E. coli Inner Membrane
Stanley B, Engelman D. Isolation and Identification of Membrane Protein Oligomers from the E. coli Inner Membrane. The FASEB Journal 2006, 20: lb76-lb77. DOI: 10.1096/fasebj.20.5.lb76-d.Peer-Reviewed Original ResearchMembrane protein oligomersMembrane proteinsOligomeric complexesHelical membrane protein structuresNatural bilayersProtein oligomersE. coli inner membraneMembrane protein structuresMembrane protein complexesProtein complex associationsAssembly of proteinsF0 subunitsProtein complexesTransmembrane domainATP synthaseInner membraneFunctional complexProtein movementTransporter complexProtein structureFunctional studiesProtein orientationProteinComplex formationMembraneph‐Triggered Transport of Molecules into Cells by Transmembrane Helix Insertion
Engelman D, Andreev O, Reshetnyak Y. ph‐Triggered Transport of Molecules into Cells by Transmembrane Helix Insertion. The FASEB Journal 2006, 20: a457-a457. DOI: 10.1096/fasebj.20.4.a457-b.Peer-Reviewed Original ResearchC-terminusTransmembrane helix insertionActin cytoskeletonHelix insertionPlasma membraneTransbilayer helicesTarget cellsCell contractilityBiophysical measurementsCancer cellsDisulfide linksCytoplasmCellsWater-soluble peptidesDiseased tissuesPeptidesMembraneAcidic pHCytoskeletonFluorescent dyeHelixPhalloidinAcidic environmentMoleculesInjection of molecules
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
1996
Crossing the Hydrophobic Barrier--Insertion of Membrane Proteins
Engelman D. Crossing the Hydrophobic Barrier--Insertion of Membrane Proteins. Science 1996, 274: 1850-1851. PMID: 8984645, DOI: 10.1126/science.274.5294.1850.Peer-Reviewed Original Research
1986
Reformation of crystalline purple membrane from purified bacteriorhodopsin fragments.
Popot J, Trewhella J, Engelman D. Reformation of crystalline purple membrane from purified bacteriorhodopsin fragments. The EMBO Journal 1986, 5: 3039-3044. PMID: 3792305, PMCID: PMC1167258, DOI: 10.1002/j.1460-2075.1986.tb04603.x.Peer-Reviewed Original ResearchLocalization 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 ResearchOn the Folding of Bacteriorhodopsin
Engelman D. On the Folding of Bacteriorhodopsin. 1986, 167-172. DOI: 10.1007/978-1-4684-8410-6_18.Peer-Reviewed Original Research
1984
Neutron Diffraction Studies of Bacteriorhodopsin Structure
Trewhella J, Gogol E, Zaccai G, Engelman D. Neutron Diffraction Studies of Bacteriorhodopsin Structure. Basic Life Sciences 1984, 227-246. DOI: 10.1007/978-1-4899-0375-4_14.Peer-Reviewed Original ResearchPlasma membraneSingle protein speciesVertebrate visual pigmentsProtein speciesPurple membraneMembrane bilayerBacteriorhodopsin structureSpecialized membraneProsthetic groupElectrochemical gradientSpecialized regionsStrong pigmentationDiffraction studiesVisual pigmentsHalobacterium halobiumX-ray diffraction studiesVisible light energyLight energyMembraneRetinal prosthetic groupLow ionic strengthSpace group P3Packing arrangementIonic strengthBacteriorhodopsin
1982
[11] The identification of helical segments in the polypeptide chain of bacteriorhodopsin
Engelman D, Goldman A, Steitz T. [11] The identification of helical segments in the polypeptide chain of bacteriorhodopsin. Methods In Enzymology 1982, 88: 81-88. DOI: 10.1016/0076-6879(82)88014-2.Peer-Reviewed Original ResearchLysine amino groupsAqueous surfaceAqueous environmentAmino groupsModification of interestPurple membrane fragmentsElectron microscopyReagentsHelical segmentsMoleculesBacteriorhodopsin structureHelical regionSingle lysineSoluble enzymePolypeptide chainCyanogen bromide fragmentsDerivitizationProteolytic enzymesKind of modificationHelixMembraneMembrane fragmentsComplexesAminoModification
1980
Bacteriorhodopsin is an inside-out protein.
Engelman D, Zaccai G. Bacteriorhodopsin is an inside-out protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 5894-5898. PMID: 6934521, PMCID: PMC350178, DOI: 10.1073/pnas.77.10.5894.Peer-Reviewed Original ResearchConceptsAmino acid sequenceSingle bacteriorhodopsin moleculePurple membrane structureAcid sequenceAlpha-helixBacteriorhodopsin moleculesSoluble proteinBiosynthetic incorporationBacteriorhodopsin structureAmino acidsHalobacterium halobiumProteinMembrane structureValineMolecular interiorPurple membranePhenylalanineDifference Fourier techniquesLipid regionsHelixHalobiumMoleculesSequenceBacteriorhodopsinMembrane
1972
The molecular structure of the membrane of Acholeplasma laidlawii
Engelman D. The molecular structure of the membrane of Acholeplasma laidlawii. Chemistry And Physics Of Lipids 1972, 8: 298-302. PMID: 5041943, DOI: 10.1016/0009-3084(72)90058-8.Peer-Reviewed Original Research
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 comparisonMeasurementsMembraneDiffraction
1968
Characterization of the plasma membrane of Mycoplasma laidlawii. IV. Structure and composition of membrane and aggregated components
Engelman D, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. IV. Structure and composition of membrane and aggregated components. Biochimica Et Biophysica Acta 1968, 150: 385-396. PMID: 5650391, DOI: 10.1016/0005-2736(68)90137-5.Peer-Reviewed Original ResearchCharacterization of the plasma membrane of Mycoplasma laidlawii. III. The formation and aggregation of small lipoprotein structures derived from sodium dodecyl sulfate-solubilized membrane components
Engelman D, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. III. The formation and aggregation of small lipoprotein structures derived from sodium dodecyl sulfate-solubilized membrane components. Biochimica Et Biophysica Acta 1968, 150: 376-384. PMID: 5650390, DOI: 10.1016/0005-2736(68)90136-3.Peer-Reviewed Original ResearchConceptsMembrane componentsSucrose density gradient centrifugationPlasma membraneSame proteinMycoplasma laidlawiiAnalytical ultracentrifugationDensity gradient centrifugationBuoyant densityGradient centrifugationProteinLipoprotein structureProtein ratioDivalent cationsLipoprotein aggregatesMembraneLarge aggregatesM Mg2LaidlawiiAggregatesLipidsUltracentrifugationSingle peak
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 preparationsProteinCharacterizationLipidsPropertiesUltracentrifugation