2001
Conversion of Phospholamban into a Soluble Pentameric Helical Bundle †
Li H, Cocco M, Steitz T, Engelman D. Conversion of Phospholamban into a Soluble Pentameric Helical Bundle †. Biochemistry 2001, 40: 6636-6645. PMID: 11380258, DOI: 10.1021/bi0026573.Peer-Reviewed Original ResearchConceptsMembrane proteinsLipid-exposed surfaceMembrane protein phospholambanLaser lightX-ray scatteringTransmembrane domainHelical bundleWild-type phospholambanOligomeric stateNative phospholambanPolar residuesSimilar foldHydrophobic residuesSoluble proteinReticulum membraneSmall-angle X-ray scatteringHelical pentamersProtein phospholambanSoluble variantProteinNatural proteinsNMR experimentsNative contactsMultiangle laser lightSarcoplasmic reticulum membranes
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
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
1993
Mutations can cause large changes in the conformation of a denatured protein.
Flanagan J, Kataoka M, Fujisawa T, Engelman D. Mutations can cause large changes in the conformation of a denatured protein. Biochemistry 1993, 32: 10359-70. PMID: 8399179, DOI: 10.1021/bi00090a011.Peer-Reviewed Original ResearchConceptsAmino acid substitutionsPolypeptide chainSecondary structureCoil-like polymerAcid substitutionsCircular dichroism spectroscopySmall-angle X-ray scatteringSingle amino acid substitutionCarboxyl-terminal deletionsPersistent secondary structureResidual secondary structureX-ray scatteringUseful model systemDelta polypeptideSolvent conditionsDichroism spectroscopyConformational distributionCarboxyl terminusNative nucleaseRandom polymersAmino acidsSingle substitutionPolymersStaphylococcal nucleaseGlobular proteins
1992
Truncated staphylococcal nuclease is compact but disordered.
Flanagan J, Kataoka M, Shortle D, Engelman D. Truncated staphylococcal nuclease is compact but disordered. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 748-752. PMID: 1731350, PMCID: PMC48316, DOI: 10.1073/pnas.89.2.748.Peer-Reviewed Original ResearchConceptsComplete folding pathwayWild-type levelsCarboxyl-terminal deletionsSecondary structural featuresNative-like conformationPersistent secondary structureProtein foldsCarboxyl terminusFolding pathwaysPolypeptide chainSecondary structureAmino acidsStaphylococcal nucleaseSmall-angle X-rayNuclear magnetic resonanceCircular dichroismPhysiological conditionsNucleasePotent inhibitorDeletionSolvent exclusionMolecules resultsStructural featuresPresence of calciumRibosomes
1985
Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering.
Seaton B, Head J, Engelman D, Richards F. Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering. Biochemistry 1985, 24: 6740-3. PMID: 4074724, DOI: 10.1021/bi00345a002.Peer-Reviewed Original Research
1979
Yeast hexokinase in solution exhibits a large conformational change upon binding glucose or glucose 6-phosphate.
McDonald R, Steitz T, Engelman D. Yeast hexokinase in solution exhibits a large conformational change upon binding glucose or glucose 6-phosphate. Biochemistry 1979, 18: 338-42. PMID: 369601, DOI: 10.1021/bi00569a017.Peer-Reviewed Original Research
1975
Determination 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