2000
Interhelical hydrogen bonding drives strong interactions in membrane proteins
Xiao Zhou F, Cocco M, Russ W, Brunger A, Engelman D. Interhelical hydrogen bonding drives strong interactions in membrane proteins. Nature Structural & Molecular Biology 2000, 7: 154-160. PMID: 10655619, DOI: 10.1038/72430.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAsparagineCell MembraneChloramphenicol O-AcetyltransferaseCircular DichroismDetergentsDimerizationDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelFungal ProteinsGlycophorinsHydrogen BondingLeucine ZippersMagnetic Resonance SpectroscopyMembrane ProteinsMicellesMicrococcal NucleaseMolecular Sequence DataPeptidesProtein ConformationProtein KinasesProtein Structure, SecondaryRecombinant ProteinsSaccharomyces cerevisiae ProteinsConceptsMembrane proteinsHelix associationTransmembrane α-helicesIntegral membrane proteinsInterhelical hydrogen bondingModel transmembrane helixTransmembrane helicesMembrane helicesGCN4 leucine zipperLeucine zipperPolar residuesSoluble proteinHydrophobic leucineΑ-helixBiological membranesProteinHelixNon-specific interactionsValine (HAV) sequenceMembraneZipperFoldingMotifAsparagineResidues
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 associatesBilayersAssessment 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
Coassembly 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
1994
Specificity and promiscuity in membrane helix interactions
Lemmon M, Engelman D. Specificity and promiscuity in membrane helix interactions. FEBS Letters 1994, 346: 17-20. PMID: 8206151, DOI: 10.1016/0014-5793(94)00467-6.Peer-Reviewed Original ResearchSpecificity and promiscuity in membrane helix interactions
Lemmon M, Engelman D. Specificity and promiscuity in membrane helix interactions. Quarterly Reviews Of Biophysics 1994, 27: 157-218. PMID: 7984776, DOI: 10.1017/s0033583500004522.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsTransmembrane α-helicesMembrane proteinsΑ-helixMembrane protein foldingMembrane-spanning portionTransmembrane helix associationHelix-helix interactionsParticular helicesProtein foldingHelix associationHelix interactionsProsthetic groupLipid bilayersCharge-charge interactionsStereochemical fitFoldingProteinAccessible statesSpecificityOligomerizationInteractionPromiscuityHelixAssemblyA dimerization motif for transmembrane α–helices
Lemmon M, Treutlein H, Adams P, Brünger A, Engelman D. A dimerization motif for transmembrane α–helices. Nature Structural & Molecular Biology 1994, 1: 157-163. PMID: 7656033, DOI: 10.1038/nsb0394-157.Peer-Reviewed Original ResearchConceptsTransmembrane α-helicesHydrophobic transmembrane α-helicesSpecific helix-helix interactionsΑ-helixIntegral membrane proteinsHelix-helix interactionsHelix-helix interfaceDimerization motifSpecific dimerizationMembrane proteinsHelix associationFunctional analysisAmino acidsSuch motifsLipid bilayersMotifParticular motifsFoldingDimerizationSuch interactionsComplex membranesProteinOligomerizationVariety of systemsInteraction
1992
Forces involved in the assembly and stabilization of membrane proteins1
Cramer W, Engelman D, Von Heijne G, Rees D. Forces involved in the assembly and stabilization of membrane proteins1. The FASEB Journal 1992, 6: 3397-3402. PMID: 1464373, DOI: 10.1096/fasebj.6.15.1464373.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsHelix-helix interactionsMembrane proteinsIntegral membrane protein complexMembrane protein complexesMembrane-spanning domainsBacterial inner membraneSpecific dimer formationCytochrome b6f complexPolarity of residuesChloroplast thylakoid membranesWater-soluble proteinsProtein complexesReconstitution of bacteriorhodopsinHydrophobic subunitsInner membraneBacterial porinsB6f complexThylakoid membranesSuch polypeptidesBasic residuesProton translocationTrans sidePhotosynthetic reaction centersTrans-membrane orientationHelix-helix interactions inside lipid bilayers
Lemmon M, Engelman D. Helix-helix interactions inside lipid bilayers. Current Opinion In Structural Biology 1992, 2: 511-518. PMCID: PMC7133266, DOI: 10.1016/0959-440x(92)90080-q.Peer-Reviewed Original ResearchTransmembrane α-helicesHelix-helix interactionsΑ-helixSingle transmembrane α-helixMechanism of transmembraneIntegral membrane proteinsNumber of proteinsMembrane-bound receptorsTransmembrane helicesInterhelical salt bridgesMembrane proteinsSoluble proteinSuch oligomerizationEndoplasmic reticulumHydrophobic anchorSuch helicesProteinLipid bilayersSalt bridgePacking interactionsOligomerizationSpecific interactionsCrystallographic studiesHelixGolgi
1990
Membrane protein folding and oligomerization: the two-stage model.
Popot J, Engelman D. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 1990, 29: 4031-7. PMID: 1694455, DOI: 10.1021/bi00469a001.Peer-Reviewed Original ResearchConceptsMembrane protein foldingIntegral membrane proteinsMembrane proteinsProtein foldingMembrane protein subunitsTransmembrane segmentsTransmembrane structureSequence dataProtein subunitsVariety of functionsAqueous channelsLipid bilayersFoldingProteinSubunitsOligomerizationAssemblyFragmentsBilayersMEMBRANE PROTEIN MODELS: POSSIBILITIES AND PROBABILITIES
POPOT J, ENGELMAN D. MEMBRANE PROTEIN MODELS: POSSIBILITIES AND PROBABILITIES. 1990, 147-151. DOI: 10.1016/b978-1-85166-512-9.50019-4.Peer-Reviewed Original ResearchThe "microassembly" of integral membrane proteins: applications & implications.
Popot J, Engelman D, Zaccai G, de Vitry C. The "microassembly" of integral membrane proteins: applications & implications. Progress In Clinical And Biological Research 1990, 343: 237-62. PMID: 2198582.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsFunctional integral membrane proteinsMost integral membrane proteinsSingle transmembrane alpha-helixInner membrane complexTransmembrane alpha-helixAutonomous folding domainsInner membraneIntegral subunitThree-dimensional structureTransmembrane regionSequence dataMembrane complexAlpha-helixExtensive rearrangementTertiary structureProteinPolypeptideLipid phasePossible roleOrganellesBiosynthesisSubunitsLocal interactions
1988
Bacteriorhodopsin in and out of Shape: Experimental Evidence in Favor of a Two-Stage Mechanism for Integral Membrane Protein Folding
Popot J, Engelman D. Bacteriorhodopsin in and out of Shape: Experimental Evidence in Favor of a Two-Stage Mechanism for Integral Membrane Protein Folding. Jerusalem Symposia 1988, 21: 381-398. DOI: 10.1007/978-94-009-3075-9_25.Peer-Reviewed Original ResearchIntegral membrane proteinsMembrane proteinsHelical integral membrane proteinsIntegral membrane protein foldingIntegral membrane protein bacteriorhodopsinMembrane protein foldingTransmembrane α-helicesMembrane protein bacteriorhodopsinTransmembrane helicesProtein foldingRenaturation experimentsVesicle fusionExtensive rearrangementNative proteinPolypeptide chainΑ-helixSequence segmentsLipid vesiclesProtein bacteriorhodopsinProteolytic fragmentsProteinFoldingHelixLipid phaseBacteriorhodopsin
1987
Folding of Integral Membrane Proteins: Renaturation Experiments with Bacteriorhodopsin Support a Two-Stage Mechanism
Popot J, Engelman D. Folding of Integral Membrane Proteins: Renaturation Experiments with Bacteriorhodopsin Support a Two-Stage Mechanism. 1987, 345-346. DOI: 10.1007/978-1-4613-1941-2_48.Peer-Reviewed Original Research
1981
The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
Engelman D, Steitz T. The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis. Cell 1981, 23: 411-422. PMID: 7471207, DOI: 10.1016/0092-8674(81)90136-7.Peer-Reviewed Original ResearchConceptsMembrane proteinsSecreted proteinsIntegral membrane proteinsHydrophobic leader peptideSecretion of proteinsHelical hairpinSpecific membrane receptorsPolypeptide sequenceSecond helixLeader peptideTransport proteinsLipid environmentTerminal helixN-terminusSpontaneous insertionMembrane receptorsHairpin structurePolypeptide structureProteinHelixHairpinHydrophobic interiorOnly alphaNonpolar sequencesHydrophobic portion