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