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
1995
Small angle x-ray scattering studies of magnetically oriented lipid bilayers
Hare B, Prestegard J, Engelman D. Small angle x-ray scattering studies of magnetically oriented lipid bilayers. Biophysical Journal 1995, 69: 1891-1896. PMID: 8580332, PMCID: PMC1236422, DOI: 10.1016/s0006-3495(95)80059-7.Peer-Reviewed Original ResearchConceptsNuclear magnetic resonanceLipid bilayersMembrane-associated moleculesBilayer thicknessLipid particlesSmall-angle X-rayX-ray scatteringAngle X-rayNMR dataDLPC vesiclesOrientational parametersX-ray solutionMolar ratioPhospholipid moleculesStructural studiesOrientational energyPhospholipid bilayersAnalogue 3MoleculesBilayersInterparticle spacingX-rayMagnetic resonanceParticlesComplexes
1979
Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase.
Pickover C, McKay D, Engelman D, Steitz T. Substrate binding closes the cleft between the domains of yeast phosphoglycerate kinase. Journal Of Biological Chemistry 1979, 254: 11323-11329. PMID: 387770, DOI: 10.1016/s0021-9258(19)86488-8.Peer-Reviewed Original ResearchConceptsYeast phosphoglycerate kinasePhosphoglycerate kinaseConformational changesTernary complexSubstrate bindingHinge motionKinaseSubstrate MgATPCleft closureSmall-angle X-raySeparate bindingRadius of gyrationAngle X-rayMgATPBindingApparent similarityComplexesCleftEnzymeObserved changesHexokinaseGyration decreasesDomainSimilarity