2000
Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions11Edited by G. von Heijne
Senes A, Gerstein M, Engelman D. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions11Edited by G. von Heijne. Journal Of Molecular Biology 2000, 296: 921-936. PMID: 10677292, DOI: 10.1006/jmbi.1999.3488.Peer-Reviewed Original ResearchAmino Acid MotifsAmino Acid SubstitutionAmino Acids, Branched-ChainBiasBinding SitesCell MembraneDatabases, FactualDimerizationGlycineGlycophorinsIsoleucineMathematicsMembrane ProteinsModels, MolecularMolecular WeightOdds RatioPliabilityProtein FoldingProtein Structure, SecondaryThermodynamicsValine
1999
A 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
1998
A solution SAXS study of borrelia burgdorferi OspA, a protein containing a single‐layer β‐sheet
Bu Z, Engelman D, Koide S. A solution SAXS study of borrelia burgdorferi OspA, a protein containing a single‐layer β‐sheet. Protein Science 1998, 7: 2681-2683. PMID: 9865964, PMCID: PMC2143892, DOI: 10.1002/pro.5560071223.Peer-Reviewed Original ResearchConceptsCrystal structureSingle-layer β-sheetPredominant solution conformationEarlier NMR studiesAngle X-ray Scattering StudySmall-angle X-ray scattering (SAXS) studiesRadius of gyrationNMR studiesSolution conformationX-ray scattering studyStable structureSAXS experimentΒ-sheetLocal structureGlobal conformationScattering StudyUnusual structureBorrelia burgdorferi outer surface protein ABeta topologyConformationBorrelia burgdorferi OspAC-terminal domainSingle layerStructureNMR
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
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
1969
Surface Area per Lipid Molecule in the Intact Membrane of the Human Red Cell
ENGELMAN D. Surface Area per Lipid Molecule in the Intact Membrane of the Human Red Cell. Nature 1969, 223: 1279-1280. PMID: 5811911, DOI: 10.1038/2231279a0.Peer-Reviewed Original Research