Monomer-oligomer equilibrium of bacteriorhodopsin in reconstituted proteoliposomes. A freeze-fracture electron microscope study.
作者： T Gulik-Krzywicki , M Seigneuret , J L Rigaud
DOI: 10.1016/S0021-9258(18)47766-6
关键词:
摘要: An improved freeze-fracture electron microscope procedure has been developed and applied to the study of association bacteriorhodopsin in large proteoliposomes reconstituted by reverse-phase evaporation with egg lecithin. Due accuracy resolution this procedure, intramembrane particles, diameter which (4.5 nm) closely matched that monomer, could be observed at high lipid protein ratios (greater than or equal 40 w/w). At lower ratios, larger particles (diameter 7.5 progressively appeared, resulting bimodal particle size distributions up a ratio 1, where were sole species present. These interpreted as corresponding oligomers. Because homogeneity proteoliposomes, accurate density measurements performed. confirmed occurrence ratio-dependent monomer-oligomer equilibrium further allowed us identify oligomer trimer tetramer. In complementary experiments, it was found monomer had identical visible CD spectra light-induced proton pumping rates. However, increase passive leak rate associated formation. The appearance these oligomers may important first step formation two-dimensional crystals bacteriorhodopsin.
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