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
2000
A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering11Edited by P. E. Wright
Bu Z, Neumann D, Lee S, Brown C, Engelman D, Han C. A view of dynamics changes in the molten globule-native folding step by quasielastic neutron scattering11Edited by P. E. Wright. Journal Of Molecular Biology 2000, 301: 525-536. PMID: 10926525, DOI: 10.1006/jmbi.2000.3978.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCattleLactalbuminModels, MolecularNeutronsProtein FoldingProtein Structure, SecondaryScattering, RadiationConceptsVibrational motionDiffusive motionPicosecond time scaleQuasielastic neutron scatteringSuch collective motionLength scalesPotential barrierQuasielastic scattering intensityCorrelation lengthJump motionShort length scalesBovine alpha-lactalbuminNeutron scatteringMolten globuleScattering intensityLong length scalesCollective motionMean-square amplitudesAtom clustersHigh-frequency motionsMolten globule stateNon-exchangeable protonsCluster sizeFrequency motionsProtein dynamicsDesign of single-layer β-sheets without a hydrophobic core
Koide S, Huang X, Link K, Koide A, Bu Z, Engelman D. Design of single-layer β-sheets without a hydrophobic core. Nature 2000, 403: 456-460. PMID: 10667801, DOI: 10.1038/35000255.Peer-Reviewed Original ResearchConceptsSingle-layer β-sheetΒ-sheetHydrophobic coreΒ-sheet segmentsProtein foldingHydrogen-deuterium exchangeOuter surface protein AΒ-sheet structureChemical denaturationSmall-angle X-rayProtein AFoldingMain thermodynamic driving forceSurface protein ABorrelia burgdorferiNuclear magnetic resonanceThermodynamic driving forceMisfoldingNonpolar moietiesHydrophobic effectSolvent resultsProteinAdjacent unitsDenaturationVariants
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-dodecylMultistep Denaturation of Borrelia burgdorferi OspA, a Protein Containing a Single-Layer β-Sheet †
Koide S, Bu Z, Risal D, Pham T, Nakagawa T, Tamura A, Engelman D. Multistep Denaturation of Borrelia burgdorferi OspA, a Protein Containing a Single-Layer β-Sheet †. Biochemistry 1999, 38: 4757-4767. PMID: 10200164, DOI: 10.1021/bi982443+.Peer-Reviewed Original ResearchConceptsSolution small-angle X-ray scatteringChemical shift differencesSingle-layer β-sheetSignificant kinetic barrierSmall-angle X-ray scatteringHeteronuclear NMR spectroscopyDifferential scanning calorimetryNMR spectroscopyRadius of gyrationX-ray scatteringDenaturation reactionNMR measurementsShift differencesKinetic barrierRigid moleculesScanning calorimetrySAXS measurementsΒ-sheetCooperative transitionReactionLys residuesBorrelia burgdorferi OspANative proteinBeta-sheet segmentThermal denaturation reaction
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
1997
Assessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering11Edited by M. F. Moody
Hunt J, McCrea P, Zaccaı̈ G, Engelman D. Assessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering11Edited by M. F. Moody. Journal Of Molecular Biology 1997, 273: 1004-1019. PMID: 9367787, DOI: 10.1006/jmbi.1997.1330.Peer-Reviewed Original ResearchConceptsMembrane protein complexesIntegral membrane proteinsProtein complexesMembrane proteinsIntegral membrane protein complexPhospholipid vesiclesSmall unilamellar phospholipid vesiclesUnilamellar phospholipid vesiclesMolecular massF. MoodySpatial arrangementNon-ionic detergentIndividual complexesVesiclesModel systemMonomeric bacteriorhodopsinProteinUnknown scopeComplexesAggregation stateRadius of gyrationBacteriorhodopsinDetergentsBilayersTwo EGF molecules contribute additively to stabilization of the EGFR dimer
Lemmon M, Bu Z, Ladbury J, Zhou M, Pinchasi D, Lax I, Engelman D, Schlessinger J. Two EGF molecules contribute additively to stabilization of the EGFR dimer. The EMBO Journal 1997, 16: 281-294. PMID: 9029149, PMCID: PMC1169635, DOI: 10.1093/emboj/16.2.281.Peer-Reviewed Original ResearchConceptsEpidermal growth factorReceptor dimerizationEGF moleculesPrecise molecular detailsHuman growth hormone receptorReceptor-receptor interactionsGrowth factorInterferon-gamma receptorEGFR dimersSignaling eventsMolecular detailsReceptor oligomerizationGrowth hormone receptorExtracellular domainEGFR familyCell surfaceMonomer bindsSubsequent associationDimerizationHormone receptorsTitration calorimetrySmall-angle X-ray scatteringBindingReceptorsMultivalent binding
1996
A Zinc-binding Domain Involved in the Dimerization of RAG1
Rodgers K, Bu Z, Fleming K, Schatz D, Engelman D, Coleman J. A Zinc-binding Domain Involved in the Dimerization of RAG1. Journal Of Molecular Biology 1996, 260: 70-84. PMID: 8676393, DOI: 10.1006/jmbi.1996.0382.Peer-Reviewed Original ResearchConceptsRecombination-activating gene 1Zinc-binding motifDimerization domainZinc fingerProtein-protein interactionsLymphoid-specific genesN-terminal thirdZinc finger sequencesAmino acid residuesC3HC4 motifRAG1 sequencesRAG1 proteinTerminal domainHomodimer formationAcid residuesBiophysical techniquesGene 1Energetics of associationMonomeric subunitsMotifProteinFinger sequencesSequenceC3HC4Zinc ions
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 ResearchMeSH KeywordsBiophysical PhenomenaBiophysicsCholic AcidsDetergentsLipid BilayersMagnetic Resonance SpectroscopyMagneticsPhosphatidylcholinesScattering, RadiationX-RaysConceptsNuclear 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
1991
Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly alpha-helical conformation.
Kataoka M, Head J, Persechini A, Kretsinger R, Engelman D. Small-angle X-ray scattering studies of calmodulin mutants with deletions in the linker region of the central helix indicate that the linker region retains a predominantly alpha-helical conformation. Biochemistry 1991, 30: 1188-92. PMID: 1991098, DOI: 10.1021/bi00219a004.Peer-Reviewed Original ResearchConceptsLinker regionCentral helixCalcium-dependent conformational changeWild-type proteinCentral linker regionSmall-angle X-rayAlpha-helical conformationGlu-84Calmodulin mutantsMutant formsGlu-83Wild typeMutantsNative proteinConformational changesCalmodulinProteinSer-81DeletionPresence of Ca2Binding of melittinSignificant size changesGlobular conformationRadius of gyrationHelix
1989
Tertiary structure of bacteriorhodopsin Positions and orientations of helices A and B in the structural map determined by neutron diffraction
Popot J, Engelman D, Gurel O, Zaccaï G. Tertiary structure of bacteriorhodopsin Positions and orientations of helices A and B in the structural map determined by neutron diffraction. Journal Of Molecular Biology 1989, 210: 829-847. PMID: 2614846, DOI: 10.1016/0022-2836(89)90111-3.Peer-Reviewed Original Research
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 Research
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
1984
Neutron scattering shows that cytochrome b5 penetrates deeply into the lipid bilayer
Gogol E, Engelman D. Neutron scattering shows that cytochrome b5 penetrates deeply into the lipid bilayer. Biophysical Journal 1984, 46: 491-495. PMID: 6498267, PMCID: PMC1435021, DOI: 10.1016/s0006-3495(84)84046-1.Peer-Reviewed Original ResearchPositions of proteins S14, S18 and S20 in the 30 S ribosomal subunit of Escherichia coli
Ramakrishnan V, Capel M, Kjeldgaard M, Engelman D, Moore P. Positions of proteins S14, S18 and S20 in the 30 S ribosomal subunit of Escherichia coli. Journal Of Molecular Biology 1984, 174: 265-284. PMID: 6371250, DOI: 10.1016/0022-2836(84)90338-3.Peer-Reviewed Original ResearchMeSH KeywordsEscherichia coliMacromolecular SubstancesModels, BiologicalMonte Carlo MethodNeutronsRibosomal ProteinsRibosomesScattering, RadiationNeutron 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 ResearchMeSH KeywordsBacterial ProteinsEscherichia coliMathematicsModels, MolecularMolecular WeightNeutronsProtein ConformationRibosomal ProteinsRibosomesScattering, RadiationInelastic Neutron Scattering Studies of Hexokinase in Solution
Engelman D, Dianoux A, Cusack S, Jacrot B. Inelastic Neutron Scattering Studies of Hexokinase in Solution. Basic Life Sciences 1984, 27: 365-380. PMID: 6712571, DOI: 10.1007/978-1-4899-0375-4_22.Peer-Reviewed Original ResearchConceptsNeutron scatteringInelastic Neutron Scattering StudyInelastic neutron scatteringInstitute Laue-LangevinNeutron Scattering StudyBiological macromoleculesMolecular dynamicsInelastic scatteringExcited modesScattering StudyScatteringSuch measurementsSuch experimentsDynamic propertiesMacromoleculesSolutionProperties