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
1994
Rotational orientation of transmembrane α-helices in bacteriorhodopsin A neutron diffraction study
Samatey F, Zaccaï G, Engelman D, Etchebest C, Popot J. Rotational orientation of transmembrane α-helices in bacteriorhodopsin A neutron diffraction study. Journal Of Molecular Biology 1994, 236: 1093-1104. PMID: 8120889, DOI: 10.1016/0022-2836(94)90014-0.Peer-Reviewed Original Research
1992
BACTERIORHODOPSIN RECONSTITUTED FROM TWO INDIVIDUAL HELICES AND THE COMPLEMENTARY FIVE‐HELIX FRAGMENT IS PHOTOACTIVE
Kataoka M, Kahn T, Tsujiuchi Y, Engelman D, Tokunaga F. BACTERIORHODOPSIN RECONSTITUTED FROM TWO INDIVIDUAL HELICES AND THE COMPLEMENTARY FIVE‐HELIX FRAGMENT IS PHOTOACTIVE. Photochemistry And Photobiology 1992, 56: 895-901. PMID: 1492135, DOI: 10.1111/j.1751-1097.1992.tb09710.x.Peer-Reviewed Original ResearchThermodynamic measurements of the contributions of helix-connecting loops and of retinal to the stability of bacteriorhodopsin.
Kahn T, Sturtevant J, Engelman D. Thermodynamic measurements of the contributions of helix-connecting loops and of retinal to the stability of bacteriorhodopsin. Biochemistry 1992, 31: 8829-39. PMID: 1390670, DOI: 10.1021/bi00152a020.Peer-Reviewed Original ResearchBacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment.
Kahn T, Engelman D. Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment. Biochemistry 1992, 31: 6144-51. PMID: 1627558, DOI: 10.1021/bi00141a027.Peer-Reviewed Original ResearchConceptsStable transmembrane helixSecond helical segmentX-ray diffractionCovalent connectionAbsorption spectroscopyTwo-dimensional crystalsIndependent folding domainsBacteriorhodopsinHelical segmentsNative structureHelixSpectroscopyPeptidesDiffractionTransmembrane helicesMoleculesCrystalsFragmentsMaterialsStructure
1991
Structure-function studies of bacteriorhodopsin XV. Effects of deletions in loops B-C and E-F on bacteriorhodopsin chromophore and structure
Gilles-Gonzalez M, Engelman D, Khorana H. Structure-function studies of bacteriorhodopsin XV. Effects of deletions in loops B-C and E-F on bacteriorhodopsin chromophore and structure. Journal Of Biological Chemistry 1991, 266: 8545-8550. PMID: 2022666, DOI: 10.1016/s0021-9258(18)93009-7.Peer-Reviewed Original Research
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 ResearchMeSH KeywordsBacteriorhodopsinsIon ChannelsLipid BilayersMembrane ProteinsModels, ChemicalProtein ConformationSolubilityConceptsMembrane protein foldingIntegral membrane proteinsMembrane proteinsProtein foldingMembrane protein subunitsTransmembrane segmentsTransmembrane structureSequence dataProtein subunitsVariety of functionsAqueous channelsLipid bilayersFoldingProteinSubunitsOligomerizationAssemblyFragmentsBilayersThe "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
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
1987
Refolding of bacteriorhodopsin in lipid bilayers A thermodynamically controlled two-stage process
Popot J, Gerchman S, Engelman D. Refolding of bacteriorhodopsin in lipid bilayers A thermodynamically controlled two-stage process. Journal Of Molecular Biology 1987, 198: 655-676. PMID: 3430624, DOI: 10.1016/0022-2836(87)90208-7.Peer-Reviewed Original ResearchConceptsLipid vesiclesAbsence of retinalAlpha-helical structureStable transmembrane helixPurple membrane latticeTransmembrane helicesSmall lipid vesiclesCircular dichroism spectraMembrane proteinsMixture of monomersFree energy minimumDodecyl sulfate solutionVesicle fusionRenatured moleculesSame absorption spectrumCorrect refoldingMajor rearrangementsStructure of bacteriorhodopsinTertiary structureMembrane latticeAbsorption spectroscopyNeutron crystallographyFolding mechanismPartial dehydration processLipid bilayers
1986
Reformation of crystalline purple membrane from purified bacteriorhodopsin fragments.
Popot J, Trewhella J, Engelman D. Reformation of crystalline purple membrane from purified bacteriorhodopsin fragments. The EMBO Journal 1986, 5: 3039-3044. PMID: 3792305, PMCID: PMC1167258, DOI: 10.1002/j.1460-2075.1986.tb04603.x.Peer-Reviewed Original ResearchMeSH KeywordsBacteriorhodopsinsChymotrypsinHalobacteriumNeutron Activation AnalysisPeptide FragmentsProtein ConformationX-Ray DiffractionLocalization of two chymotryptic fragments in the structure of renatured bacteriorhodopsin by neutron diffraction.
Trewhella J, Popot J, Zaccaï G, Engelman D. Localization of two chymotryptic fragments in the structure of renatured bacteriorhodopsin by neutron diffraction. The EMBO Journal 1986, 5: 3045-3049. PMID: 3792306, PMCID: PMC1167259, DOI: 10.1002/j.1460-2075.1986.tb04604.x.Peer-Reviewed Original Research
1985
Stability of transmembrane regions in bacteriorhodopsin studied by progressive proteolysis
Dumont M, Trewhella J, Engelman D, Richards F. Stability of transmembrane regions in bacteriorhodopsin studied by progressive proteolysis. The Journal Of Membrane Biology 1985, 88: 233-247. PMID: 3913776, DOI: 10.1007/bf01871088.Peer-Reviewed Original ResearchConceptsMolecular weight distributionFragments of bacteriorhodopsinVisible absorption spectraX-ray diffractionX-ray diffraction patternsDiffraction patternsAqueous mediaNative purple membraneUrea-polyacrylamide gel electrophoresisWeight distributionSmall soluble peptidesAbsorption spectraHydrophobic segmentsBacteriorhodopsin sequenceAmino acid analysisHigh-pressure liquid chromotographyPolyacrylamide gel electrophoresisDigestion conditionsPurple membraneOptical absorptionSoluble peptidesBacteriorhodopsinMembrane-embedded regionsLiquid chromotographyProducts of digestion
1983
Pair distribution functions of bacteriorhodopsin and rhodopsin in model bilayers
Pearson L, Chan S, Lewis B, Engelman D. Pair distribution functions of bacteriorhodopsin and rhodopsin in model bilayers. Biophysical Journal 1983, 43: 167-174. PMID: 6616005, PMCID: PMC1329246, DOI: 10.1016/s0006-3495(83)84337-9.Peer-Reviewed Original ResearchAssignment of segments of the bacteriorhodopsin sequence to positions in the structural map
Trewhella J, Anderson S, Fox R, Gogol E, Khan S, Engelman D, Zaccai G. Assignment of segments of the bacteriorhodopsin sequence to positions in the structural map. Biophysical Journal 1983, 42: 233-241. PMID: 6871370, PMCID: PMC1329232, DOI: 10.1016/s0006-3495(83)84391-4.Peer-Reviewed Original ResearchBacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses
Lewis B, Engelman D. Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses. Journal Of Molecular Biology 1983, 166: 203-210. PMID: 6854643, DOI: 10.1016/s0022-2836(83)80006-0.Peer-Reviewed Original Research
1980
Bacteriorhodopsin is an inside-out protein.
Engelman D, Zaccai G. Bacteriorhodopsin is an inside-out protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 5894-5898. PMID: 6934521, PMCID: PMC350178, DOI: 10.1073/pnas.77.10.5894.Peer-Reviewed Original ResearchMeSH KeywordsBacteriorhodopsinsCarotenoidsHalobacteriumNeutronsProtein ConformationScattering, RadiationConceptsAmino acid sequenceSingle bacteriorhodopsin moleculePurple membrane structureAcid sequenceAlpha-helixBacteriorhodopsin moleculesSoluble proteinBiosynthetic incorporationBacteriorhodopsin structureAmino acidsHalobacterium halobiumProteinMembrane structureValineMolecular interiorPurple membranePhenylalanineDifference Fourier techniquesLipid regionsHelixHalobiumMoleculesSequenceBacteriorhodopsinMembranePath of the polypeptide in bacteriorhodopsin.
Engelman D, Henderson R, McLachlan A, Wallace B. Path of the polypeptide in bacteriorhodopsin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 2023-2027. PMID: 6929535, PMCID: PMC348643, DOI: 10.1073/pnas.77.4.2023.Peer-Reviewed Original Research