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
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 gyrationBacteriorhodopsinDetergentsBilayers
1996
Surface point mutations that significantly alter the structure and stability of a protein's denatured state
Smith C, Bu Z, Engelman D, Regan L, Anderson K, Sturtevant J. Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Science 1996, 5: 2009-2019. PMID: 8897601, PMCID: PMC2143264, DOI: 10.1002/pro.5560051007.Peer-Reviewed Original ResearchConceptsPoint mutationsDenatured stateStopped-flow fluorescenceDenaturant concentrationSolvent-exposed sitesStreptococcal protein GMutantsG mutantTertiary structureGuHCl denaturationEquilibrium intermediatesPosition 53B1 domainProteinCircular dichroismMutationsProtein GGuanidine hydrochlorideSmall-angle X-ray scatteringStructural implicationsX-ray scatteringFluorescenceThrRadius of gyrationDenaturants
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
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
1975
A neutron scattering study of the distribution of protein and RNA in the 30 S ribosomal subunit of Escherichia coli
Moore P, Engelman D, Schoenborn B. A neutron scattering study of the distribution of protein and RNA in the 30 S ribosomal subunit of Escherichia coli. Journal Of Molecular Biology 1975, 91: 101-120. PMID: 1102695, DOI: 10.1016/0022-2836(75)90374-5.Peer-Reviewed Original Research