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 ResearchLocalization 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
Assignment 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