1992
Thermodynamic 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
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