2001
Genetic selection for and molecular dynamic modeling of a protein transmembrane domain multimerization motif from a random Escherichia coli genomic library 1 1 Edited by G. von Heijne
Leeds J, Boyd D, Huber D, Sonoda G, Luu H, Engelman D, Beckwith J. Genetic selection for and molecular dynamic modeling of a protein transmembrane domain multimerization motif from a random Escherichia coli genomic library 1 1 Edited by G. von Heijne. Journal Of Molecular Biology 2001, 313: 181-195. PMID: 11601855, DOI: 10.1006/jmbi.2001.5007.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionBacteriophage lambdaBase SequenceBinding SitesCell MembraneCloning, MolecularDimerizationDNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsGenes, BacterialGenetic VectorsGenomic LibraryMembrane ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein Sorting SignalsProtein Structure, QuaternaryProtein Structure, TertiaryProtein SubunitsProtein TransportRecombinant Fusion ProteinsRepressor ProteinsViral ProteinsViral Regulatory and Accessory ProteinsConceptsTransmembrane domainTransmembrane helix-helix associationE. coli inner membraneMembrane protein structuresGenomic DNA fragmentsHelix-helix associationG. von HeijneHelix-helix interactionsSite-directed mutagenesisSixth transmembrane domainTransmembrane helicesRepressor DNAGenetic toolsInner membraneVon HeijneProtein structureDNA fragmentsGenetic selectionNovel sequencesMultimerization motifMotifSequenceHomomultimerizationDomainMutagenesis
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
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