2000
The GxxxG motif: A framework for transmembrane helix-helix association11Edited by G. von Heijne
Russ W, Engelman D. The GxxxG motif: A framework for transmembrane helix-helix association11Edited by G. von Heijne. Journal Of Molecular Biology 2000, 296: 911-919. PMID: 10677291, DOI: 10.1006/jmbi.1999.3489.Peer-Reviewed Original ResearchAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBinding SitesChloramphenicol ResistanceCloning, MolecularConsensus SequenceDatabases, FactualDimerizationDNA-Binding ProteinsEscherichia coliGlycophorinsIntracellular MembranesMembrane ProteinsModels, MolecularPeptide LibraryProtein Structure, SecondaryProtein Structure, TertiaryThermodynamicsTranscription Factors
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
Surface point mutations that significantly alter the structure and stability of a protein's denatured state
Smith C, Bu Z, Engelman D, Regan L, Anderson K, Sturtevant J. Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Science 1996, 5: 2009-2019. PMID: 8897601, PMCID: PMC2143264, DOI: 10.1002/pro.5560051007.Peer-Reviewed Original ResearchConceptsPoint mutationsDenatured stateStopped-flow fluorescenceDenaturant concentrationSolvent-exposed sitesStreptococcal protein GMutantsG mutantTertiary structureGuHCl denaturationEquilibrium intermediatesPosition 53B1 domainProteinCircular dichroismMutationsProtein GGuanidine hydrochlorideSmall-angle X-ray scatteringStructural implicationsX-ray scatteringFluorescenceThrRadius of gyrationDenaturants
1987
A Complete Mapping of the Proteins in the Small Ribosomal Subunit of Escherichia coli
Capel M, Engelman D, Freeborn B, Kjeldgaard M, Langer J, Ramakrishnan V, Schindler D, Schneider D, Schoenborn B, Sillers I, Yabuki S, Moore P. A Complete Mapping of the Proteins in the Small Ribosomal Subunit of Escherichia coli. Science 1987, 238: 1403-1406. PMID: 3317832, DOI: 10.1126/science.3317832.Peer-Reviewed Original Research
1984
Neutron Scattering and the 30 S Ribosomal Subunit of E. coli
Moore P, Engelman D, Langer J, Ramakrishnan V, Schindler D, Schoenborn B, Sillers I, Yabuki S. Neutron Scattering and the 30 S Ribosomal Subunit of E. coli. Basic Life Sciences 1984, 27: 73-91. PMID: 6370225, DOI: 10.1007/978-1-4899-0375-4_4.Peer-Reviewed Original Research
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
1978
Neutron-scattering studies of the ribosome of Escherichia coli: A provisional map of the locations of proteins S3, S4, S5, S7, S8 and S9 in the 30 S subunit
Langer J, Engelman D, Moore P. Neutron-scattering studies of the ribosome of Escherichia coli: A provisional map of the locations of proteins S3, S4, S5, S7, S8 and S9 in the 30 S subunit. Journal Of Molecular Biology 1978, 119: 463-485. PMID: 347087, DOI: 10.1016/0022-2836(78)90197-3.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBinding SitesCrystallographyEscherichia coliModels, MolecularNeutronsRibosomal ProteinsRibosomes
1976
Protein pair distance determination in the 30 S ribosomal subunit of E. coli.
Engelman D, Moore P, Schoenborn B. Protein pair distance determination in the 30 S ribosomal subunit of E. coli. Brookhaven Symposia In Biology 1976, iv20-iv37. PMID: 786445.Peer-Reviewed Original ResearchThe production of deuterated E. coli.
Moore P, Engelman D. The production of deuterated E. coli. Brookhaven Symposia In Biology 1976, v12-v23. PMID: 786448.Peer-Reviewed Original Research
1975
A neutron scattering study of the distribution of protein and RNA in the 30 S ribosomal subunit of Escherichia coli
Moore P, Engelman D, Schoenborn B. A neutron scattering study of the distribution of protein and RNA in the 30 S ribosomal subunit of Escherichia coli. Journal Of Molecular Biology 1975, 91: 101-120. PMID: 1102695, DOI: 10.1016/0022-2836(75)90374-5.Peer-Reviewed Original Research
1974
The lac Repressor Protein: Molecular Shape, Subunit Structure, and Proposed Model for Operator Interaction Based on Structural Studies of Microcrystals
Steitz T, Richmond T, Wise D, Engelman D. The lac Repressor Protein: Molecular Shape, Subunit Structure, and Proposed Model for Operator Interaction Based on Structural Studies of Microcrystals. Proceedings Of The National Academy Of Sciences Of The United States Of America 1974, 71: 593-597. PMID: 4595565, PMCID: PMC388057, DOI: 10.1073/pnas.71.3.593.Peer-Reviewed Original ResearchAsymmetry in the 50S Ribosomal Subunit of Escherichia coli
Moore P, Engelman D, Schoenborn B. Asymmetry in the 50S Ribosomal Subunit of Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1974, 71: 172-176. PMID: 4589891, PMCID: PMC387959, DOI: 10.1073/pnas.71.1.172.Peer-Reviewed Original Research
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 ResearchMeSH KeywordsAcholeplasma laidlawiiBacterial ProteinsCell MembraneCulture MediaFatty AcidsLipid MetabolismMycoplasmaTemperatureX-Ray Diffraction
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