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 vesiclesHelixFoldingBacteriorhodopsinAssessment 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
1992
Bacteriorhodopsin 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
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
1986
On the Folding of Bacteriorhodopsin
Engelman D. On the Folding of Bacteriorhodopsin. 1986, 167-172. DOI: 10.1007/978-1-4684-8410-6_18.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
1984
Neutron Diffraction Studies of Bacteriorhodopsin Structure
Trewhella J, Gogol E, Zaccai G, Engelman D. Neutron Diffraction Studies of Bacteriorhodopsin Structure. Basic Life Sciences 1984, 227-246. DOI: 10.1007/978-1-4899-0375-4_14.Peer-Reviewed Original ResearchPlasma membraneSingle protein speciesVertebrate visual pigmentsProtein speciesPurple membraneMembrane bilayerBacteriorhodopsin structureSpecialized membraneProsthetic groupElectrochemical gradientSpecialized regionsStrong pigmentationDiffraction studiesVisual pigmentsHalobacterium halobiumX-ray diffraction studiesVisible light energyLight energyMembraneRetinal prosthetic groupLow ionic strengthSpace group P3Packing arrangementIonic strengthBacteriorhodopsin
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 ResearchConceptsAmino acid sequenceSingle bacteriorhodopsin moleculePurple membrane structureAcid sequenceAlpha-helixBacteriorhodopsin moleculesSoluble proteinBiosynthetic incorporationBacteriorhodopsin structureAmino acidsHalobacterium halobiumProteinMembrane structureValineMolecular interiorPurple membranePhenylalanineDifference Fourier techniquesLipid regionsHelixHalobiumMoleculesSequenceBacteriorhodopsinMembrane