McClurg RB, Zukoski CF
Department of Chemical Engineering, University of Illinois, Urbana, Illinois, 61801
J Colloid Interface Sci. 1998 Dec 15;208(2):529-542. doi: 10.1006/jcis.1998.5858.
We use the linearized Poisson-Boltzmann equation to construct an analytical estimate of the electrostatic interaction energy for two rigid, globular proteins with arbitrary charge distributions represented by spherical multipole moments. Our analysis avoids invoking the superposition approximation and therefore is not limited to weakly interacting double layers. The interaction energy is a function of the protein properties (radii, multipole moments, and dielectric constant); the geometry (protein separation and orientations); and the solution properties (Debye screening length and dielectric constant). The proteins may be different. This is an extension of previous treatments for constant surface charge or for constant surface potential particles that are more applicable to isotropic colloids. We give example calculations for the interactions of Ribonuclease A molecules interacting in an electrolyte. These results suggest that electrostatic effects may be largely responsible for attractions between proteins, even if they are like charged. A set of routines using MATHEMATICA is available for performing the interaction energy and electrostatic potential calculations. Copyright 1998 Academic Press.
我们使用线性化的泊松-玻尔兹曼方程，对两个具有由球形多极矩表示的任意电荷分布的刚性球状蛋白质的静电相互作用能进行解析估计。我们的分析避免了调用叠加近似，因此不限于弱相互作用的双层。相互作用能是蛋白质性质（半径、多极矩和介电常数）、几何结构（蛋白质间距和取向）以及溶液性质（德拜屏蔽长度和介电常数）的函数。这两个蛋白质可以不同。这是先前对恒定表面电荷或恒定表面电位粒子处理方法的扩展，更适用于各向同性胶体。我们给出了在电解质中相互作用的核糖核酸酶A分子相互作用的示例计算。这些结果表明，即使蛋白质带相同电荷，静电效应也可能在很大程度上导致蛋白质之间的吸引力。有一组使用MATHEMATICA的程序可用于进行相互作用能和静电势的计算。版权所有1998年学术出版社。
