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
1982
[11] The identification of helical segments in the polypeptide chain of bacteriorhodopsin
Engelman D, Goldman A, Steitz T. [11] The identification of helical segments in the polypeptide chain of bacteriorhodopsin. Methods In Enzymology 1982, 88: 81-88. DOI: 10.1016/0076-6879(82)88014-2.Peer-Reviewed Original ResearchLysine amino groupsAqueous surfaceAqueous environmentAmino groupsModification of interestPurple membrane fragmentsElectron microscopyReagentsHelical segmentsMoleculesBacteriorhodopsin structureHelical regionSingle lysineSoluble enzymePolypeptide chainCyanogen bromide fragmentsDerivitizationProteolytic enzymesKind of modificationHelixMembraneMembrane fragmentsComplexesAminoModification