2000
Design 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
Multistep 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
1968
Characterization of the plasma membrane of Mycoplasma laidlawii. IV. Structure and composition of membrane and aggregated components
Engelman D, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. IV. Structure and composition of membrane and aggregated components. Biochimica Et Biophysica Acta 1968, 150: 385-396. PMID: 5650391, DOI: 10.1016/0005-2736(68)90137-5.Peer-Reviewed Original ResearchCharacterization of the plasma membrane of Mycoplasma laidlawii. III. The formation and aggregation of small lipoprotein structures derived from sodium dodecyl sulfate-solubilized membrane components
Engelman D, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. III. The formation and aggregation of small lipoprotein structures derived from sodium dodecyl sulfate-solubilized membrane components. Biochimica Et Biophysica Acta 1968, 150: 376-384. PMID: 5650390, DOI: 10.1016/0005-2736(68)90136-3.Peer-Reviewed Original ResearchConceptsMembrane componentsSucrose density gradient centrifugationPlasma membraneSame proteinMycoplasma laidlawiiAnalytical ultracentrifugationDensity gradient centrifugationBuoyant densityGradient centrifugationProteinLipoprotein structureProtein ratioDivalent cationsLipoprotein aggregatesMembraneLarge aggregatesM Mg2LaidlawiiAggregatesLipidsUltracentrifugationSingle peak
1967
Characterization of the plasma membrane of Mycoplasma laidlawii. II. Modes of aggregation of solubilized membrane components
Terry T, Engelman D, Morowitz H. Characterization of the plasma membrane of Mycoplasma laidlawii. II. Modes of aggregation of solubilized membrane components. Biochimica Et Biophysica Acta 1967, 135: 391-405. PMID: 6058126, DOI: 10.1016/0005-2736(67)90029-6.Peer-Reviewed Original Research