Sperotto M M, Mouritsen O G
Department of Structural Properties of Materials, Technical University of Denmark, Lyngby.
Biophys J. 1991 Feb;59(2):261-70. doi: 10.1016/S0006-3495(91)82219-6.
Monte Carlo simulation techniques have been applied to a statistical mechanical lattice model in order to study the coherence length for the spatial fluctuations of the lipid order parameter profiles around integral membrane proteins in dipalmitoyl phosphatidylcholine bilayers. The model, which provides a detailed description of the pure lipid bilayer main transition, incorporates hydrophobic matching between the lipid and protein hydrophobic thicknesses as a major contribution to the lipid-protein interactions in lipid membranes. The model is studied at low protein-to-lipid ratios. The temperature dependence of the coherence length is found to have a dramatic peak at the phase transition temperature. The dependence on protein circumference as well as hydrophobic length is determined and it is concluded that in some cases the coherence length is much longer than previously anticipated. The long coherence length provides a mechanism for indirect lipid-mediated protein-protein long-range attraction and hence plays an important role in regulating protein segregation.
蒙特卡罗模拟技术已应用于统计力学晶格模型，以研究二棕榈酰磷脂酰胆碱双层中整合膜蛋白周围脂质序参数分布的空间涨落的相干长度。该模型详细描述了纯脂质双层的主要转变，将脂质与蛋白质疏水厚度之间的疏水匹配作为脂质膜中脂质 - 蛋白质相互作用的主要贡献因素。该模型在低蛋白质与脂质比例下进行研究。发现相干长度的温度依赖性在相变温度处有一个显著的峰值。确定了其对蛋白质周长以及疏水长度的依赖性，并得出结论，在某些情况下，相干长度比先前预期的要长得多。长相干长度为间接脂质介导的蛋白质 - 蛋白质远程吸引提供了一种机制，因此在调节蛋白质分离中起重要作用。
