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
1990
Membrane protein folding and oligomerization: the two-stage model.
Popot J, Engelman D. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 1990, 29: 4031-7. PMID: 1694455, DOI: 10.1021/bi00469a001.Peer-Reviewed Original ResearchConceptsMembrane protein foldingIntegral membrane proteinsMembrane proteinsProtein foldingMembrane protein subunitsTransmembrane segmentsTransmembrane structureSequence dataProtein subunitsVariety of functionsAqueous channelsLipid bilayersFoldingProteinSubunitsOligomerizationAssemblyFragmentsBilayers
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