1999
TOXCAT: 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
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 orientation
1994
Specificity and promiscuity in membrane helix interactions
Lemmon M, Engelman D. Specificity and promiscuity in membrane helix interactions. FEBS Letters 1994, 346: 17-20. PMID: 8206151, DOI: 10.1016/0014-5793(94)00467-6.Peer-Reviewed Original Research
1992
Intramembrane Helix-Helix Association in Oligomerization and Transmembrane Signaling
Bormann B, Engelman D. Intramembrane Helix-Helix Association in Oligomerization and Transmembrane Signaling. Annual Review Of Biophysics 1992, 21: 223-242. PMID: 1326354, DOI: 10.1146/annurev.bb.21.060192.001255.Peer-Reviewed Original ResearchConceptsProtein foldingTransmembrane regionReceptor proteinClose contact sitesSignal transductionQuaternary structureReceptor moleculesConformational changesHelical transmembrane regionsAllosteric conformational changeHelix-helix associationConformational change modelTertiary/quaternary structureTransmembrane helicesTransmembrane domainMechanism of insertionCytoplasmic domainTransmembrane signalingContact sitesPrimary structureSecondary structureProteinOligomerizationFoldingProteolytic fragments
1988
Positions of S2, S13, S16, S17, S19 and S21 in the 30 S ribosomal subunit of Escherichia coli
Capel M, Kjeldgaard M, Engelman D, Moore P. Positions of S2, S13, S16, S17, S19 and S21 in the 30 S ribosomal subunit of Escherichia coli. Journal Of Molecular Biology 1988, 200: 65-87. PMID: 3288761, DOI: 10.1016/0022-2836(88)90334-8.Peer-Reviewed Original ResearchMeSH KeywordsEscherichia coliEscherichia coli ProteinsMacromolecular SubstancesModels, MolecularNeutronsProtein ConformationRibosomal ProteinsRibosomesScattering, Radiation
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
1984
Positions of proteins S14, S18 and S20 in the 30 S ribosomal subunit of Escherichia coli
Ramakrishnan V, Capel M, Kjeldgaard M, Engelman D, Moore P. Positions of proteins S14, S18 and S20 in the 30 S ribosomal subunit of Escherichia coli. Journal Of Molecular Biology 1984, 174: 265-284. PMID: 6371250, DOI: 10.1016/0022-2836(84)90338-3.Peer-Reviewed Original ResearchMeSH KeywordsEscherichia coliMacromolecular SubstancesModels, BiologicalMonte Carlo MethodNeutronsRibosomal ProteinsRibosomesScattering, Radiation
1981
Positions of proteins S6, S11 and S15 in the 30 S ribosomal subunit of Escherichia coli
Ramakrishnan V, Yabuki S, Sillers I, Schindler D, Engelman D, Moore P. Positions of proteins S6, S11 and S15 in the 30 S ribosomal subunit of Escherichia coli. Journal Of Molecular Biology 1981, 153: 739-760. PMID: 7040690, DOI: 10.1016/0022-2836(81)90416-2.Peer-Reviewed Original Research
1979
Small angle X-ray scattering of dimeric yeast hexokinase in solution.
McDonald R, Engelman D, Steitz T. Small angle X-ray scattering of dimeric yeast hexokinase in solution. Journal Of Biological Chemistry 1979, 254: 2942-2943. PMID: 372185, DOI: 10.1016/s0021-9258(17)30165-5.Peer-Reviewed Original ResearchMeSH KeywordsHexokinaseMacromolecular SubstancesProtein ConformationSaccharomyces cerevisiaeX-Ray Diffraction
1975
The use of x-ray scattering in the study of lipid bilayer planar organization
Engelman D. The use of x-ray scattering in the study of lipid bilayer planar organization. Biophysical Journal 1975, 15: 940-944. PMID: 1182268, PMCID: PMC1334757, DOI: 10.1016/s0006-3495(75)85871-1.Peer-Reviewed Original ResearchDetermination of Quaternary Structure by Small Angle Neutron Scattering
Engelman D, Moore P. Determination of Quaternary Structure by Small Angle Neutron Scattering. Annual Review Of Biophysics And Bioengineering 1975, 4: 219-241. PMID: 1098555, DOI: 10.1146/annurev.bb.04.060175.001251.Peer-Reviewed Original Research
1972
A New Method for the Determination of Biological Quarternary Structure by Neutron Scattering
Engelman D, Moore P. A New Method for the Determination of Biological Quarternary Structure by Neutron Scattering. Proceedings Of The National Academy Of Sciences Of The United States Of America 1972, 69: 1997-1999. PMID: 4506067, PMCID: PMC426853, DOI: 10.1073/pnas.69.8.1997.Peer-Reviewed Original ResearchMeSH KeywordsDeuteriumMacromolecular SubstancesModels, BiologicalMolecular WeightNeutronsProteinsRibosomesRNA, Ribosomal
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