Biophys J. 1986 Jun;49(6):1111-8. doi: 10.1016/S0006-3495(86)83740-7.
Reaction-center proteins of Rhodopseudomonas Sphaeroides reconstituted into phosphatidylcholine vesicles shift and broaden the fluid-gel transition of the lipid bilayer. The amount of broadening and temperature shift of the transition depend both on protein concentration and on lipid chain length. In particular, the direction of the transition temperature shift is very sensitive to lipid chain length. Electron micrographs show homogeneous protein distribution on the fluid surface whereas the solid phase contains protein aggregates the type depending on chain length. The results can qualitatively be understood in the framework of a mattress model of lipid/protein interactions in membranes.
球形红假单胞菌的反应中心蛋白重构成磷脂囊泡后会使脂质双层的流态-凝胶相变移动和变宽。变宽的程度和相变的温度移动取决于蛋白质浓度和脂质链长。特别是,相变温度移动的方向对脂质链长非常敏感。电子显微镜照片显示蛋白质在流态表面均匀分布,而固态则包含取决于链长的蛋白质聚集体。这些结果可以在脂质/蛋白质相互作用的床垫模型框架内定性地理解。