1999
Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain 11Edited by G. von Heijne
Fisher L, Engelman D, Sturgis J. Detergents modulate dimerization, but not helicity, of the glycophorin A transmembrane domain 11Edited by G. von Heijne. Journal Of Molecular Biology 1999, 293: 639-651. PMID: 10543956, DOI: 10.1006/jmbi.1999.3126.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceButyratesCircular DichroismDetergentsDimerizationEnergy TransferFluorescent DyesGlycophorinsHumansKineticsMicellesMolecular Sequence DataPeptide FragmentsPhosphorylcholineProtein Structure, SecondaryQuaternary Ammonium CompoundsSodium Dodecyl SulfateSolventsSpectrometry, FluorescenceThermodynamicsConceptsSpecific chemical interactionsFörster resonance energy transferResonance energy transferSodium dodecyl sulfateComplex solventChemical interactionFar-UV circular dichroismCircular dichroismDodecyl sulfateTransmembrane helix associationDetergent micellesHelix associationEnergy transferThermodynamic measurementsHelix formationObserved KdZwitterionic detergentSecondary structureDimerizationG. von HeijneHelix dimerizationOrders of magnitudeDetergentsTransmembrane helicesTransmembrane domain
1997
A Biophysical Study of Integral Membrane Protein Folding †
Hunt J, Earnest T, Bousché O, Kalghatgi K, Reilly K, Horváth C, Rothschild K, Engelman D. A Biophysical Study of Integral Membrane Protein Folding †. Biochemistry 1997, 36: 15156-15176. PMID: 9398244, DOI: 10.1021/bi970146j.Peer-Reviewed Original ResearchConceptsAlpha-helical integral membrane proteinsIntegral membrane proteinsMembrane proteinsIntegral membrane protein foldingMembrane protein foldingNon-native conformationsStable secondary structureCellular chaperonesBiophysical dissectionBeta-sheet structureProtein foldingIndividual polypeptidesBiophysical studiesStructure of bacteriorhodopsinTertiary structureSecondary structureReconstitution protocolsG helicesPolypeptideF helixProteinPhospholipid vesiclesHelixFoldingBacteriorhodopsinSpontaneous, pH-Dependent Membrane Insertion of a Transbilayer α-Helix †
Hunt J, Rath P, Rothschild K, Engelman D. Spontaneous, pH-Dependent Membrane Insertion of a Transbilayer α-Helix †. Biochemistry 1997, 36: 15177-15192. PMID: 9398245, DOI: 10.1021/bi970147b.Peer-Reviewed Original ResearchConceptsLipid bilayersIntegral membrane protein bacteriorhodopsinMembrane-spanning regionIntegral membrane proteinsPH-dependent membrane insertionAspartic acid residuesMembrane protein bacteriorhodopsinInsertion reactionMembrane insertionMembrane proteinsAqueous solutionHydrophobic sequenceAqueous bufferPoor solubilityAlpha-helixAcid residuesSignificant solubilityC-helixSpectroscopic assaysΑ-helixSecondary structureProtein bacteriorhodopsinNeutral pHPeptide associatesBilayers
1996
Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban
Ludlam C, Arkin I, Liu X, Rothman M, Rath P, Aimoto S, Smith S, Engelman D, Rothschild K. Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban. Biophysical Journal 1996, 70: 1728-1736. PMID: 8785331, PMCID: PMC1225141, DOI: 10.1016/s0006-3495(96)79735-7.Peer-Reviewed Original ResearchConceptsSite-directed isotope labelingLocal secondary structureIsotope labelingSecondary structureSelective ion channelsTotal reflection Fourier transformPeptide amide groupsAmide IReflection Fourier transformDeuterium/hydrogen exchangeTransmembrane domainMembrane domainsMembrane proteinsTransmembrane orientationAmino acid fragmentSpectroscopic characterizationIon channelsHydrophobic regionAmide carbonylProtein backboneCardiac muscle cellsAmide groupLipid bilayersATPase activityFourier transformCoassembly of Synthetic Segments of Shaker K+ Channel within Phospholipid Membranes †
Peled-Zehavi H, Arkin I, Engelman D, Shai Y. Coassembly of Synthetic Segments of Shaker K+ Channel within Phospholipid Membranes †. Biochemistry 1996, 35: 6828-6838. PMID: 8639634, DOI: 10.1021/bi952988t.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsOligomerization of proteinsMembrane-embedded segmentsMembrane-mimetic environmentsAlpha-helical contentAlpha-helical structureLipid/peptide molar ratioS4 regionShaker potassium channelSecondary structure studiesResonance energy transfer measurementsPhospholipid membranesZwitterionic phospholipid vesiclesTransmembrane segmentsMembrane proteinsPhospholipid milieuMimetic environmentsSynthetic segmentsFirst repeatS4 sequenceEel sodium channelS4 segmentEnergy transfer measurementsSecondary structure
1995
Structural Model of the Phospholamban Ion Channel Complex in Phospholipid Membranes
Arkin I, Rothman M, Ludlam C, Aimoto S, Engelman D, Rothschild K, Smith S. Structural Model of the Phospholamban Ion Channel Complex in Phospholipid Membranes. Journal Of Molecular Biology 1995, 248: 824-834. PMID: 7752243, DOI: 10.1006/jmbi.1995.0263.Peer-Reviewed Original ResearchConceptsSelective ion conductanceTransmembrane domainAmino acid residuesN-terminal 30 amino acid residuesAcid residuesCircular dichroismPentameric protein complexFull-length proteinC-terminal 22 amino acid residuesPhospholipid membranesIon channel complexTransmembrane helicesProtein complexesPhosphorylation sitesMembrane proteinsIon conductanceCarboxy terminusHelix bundleIon poreReticulum membraneInhibitory complexLong helixPentameric complexSecondary structureProtein
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
Intramembrane Helix-Helix Association in Oligomerization and Transmembrane Signaling
Bormann B, Engelman D. Intramembrane Helix-Helix Association in Oligomerization and Transmembrane Signaling. Annual Review Of Biophysics 1992, 21: 223-242. PMID: 1326354, DOI: 10.1146/annurev.bb.21.060192.001255.Peer-Reviewed Original ResearchConceptsProtein foldingTransmembrane regionReceptor proteinClose contact sitesSignal transductionQuaternary structureReceptor moleculesConformational changesHelical transmembrane regionsAllosteric conformational changeHelix-helix associationConformational change modelTertiary/quaternary structureTransmembrane helicesTransmembrane domainMechanism of insertionCytoplasmic domainTransmembrane signalingContact sitesPrimary structureSecondary structureProteinOligomerizationFoldingProteolytic fragmentsTruncated 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