Mouritsen O G, Bloom M
Biophys J. 1984 Aug;46(2):141-53. doi: 10.1016/S0006-3495(84)84007-2.
A thermodynamic model is proposed for describing phase diagrams of mixtures of lipid bilayers and amphiphilic proteins or polypeptides in water solution. The basic geometrical variables of the model are the thickness of the hydrophobic region of the lipid bilayer and the length of the hydrophobic region of the proteins. The model incorporates the elastic properties of the lipid bilayer and the proteins, as well as indirect and direct lipid-protein interactions expressed in terms of the geometrical variables. The concept of mismatch of the hydrophobic regions of the lipids and proteins is an important ingredient of the model. The general phase behavior is calculated using simple real solution theory. The phase behavior turns out to be quite rich and is used to discuss previous experiments on planar aggregations of proteins in phospholipid bilayers and to propose a systematic study of synthetic amphiphilic polypeptides in bilayers of different thicknesses. The model is used to interpret the influence of the lipid-protein interaction on calorimetric measurements and on local orientational order as determined by deuterium nuclear magnetic resonance.
提出了一种热力学模型，用于描述水溶液中脂质双层与两亲性蛋白质或多肽混合物的相图。该模型的基本几何变量是脂质双层疏水区域的厚度和蛋白质疏水区域的长度。该模型纳入了脂质双层和蛋白质的弹性特性，以及根据几何变量表示的间接和直接脂质 - 蛋白质相互作用。脂质和蛋白质疏水区域不匹配的概念是该模型的一个重要组成部分。使用简单的真实溶液理论计算一般相行为。结果表明相行为相当丰富，可用于讨论先前关于磷脂双层中蛋白质平面聚集的实验，并提出对不同厚度双层中合成两亲性多肽进行系统研究。该模型用于解释脂质 - 蛋白质相互作用对量热测量以及由氘核磁共振确定的局部取向有序的影响。
