ON THE CALCULATION OF ELECTROSTATIC INTERACTIONS IN PROTEINS
ON THE CALCULATION OF ELECTROSTATIC INTERACTIONS IN PROTEINS
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DOI：
10.1016/0022-2836(85)90297-9
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发表时间：
1985-01-01
影响因子：
5.6
通讯作者：
HONIG, B
中科院分区：
文献类型：
--
作者：
GILSON, MK;RASHIN, A;HONIG, B
蛋白质静电相互作用的经典处理。蛋白质被视为一个低介电常数的区域，其中嵌入了球形电荷，被高介电常数的水性溶剂包围，其中可能含有简单的电解质。完整的分析包括溶剂屏蔽，极化力，和自我的能量，这是有关的溶剂化能量的影响。公式，和样本计算力和能量，给出了特殊情况下的球形蛋白质。我们的分析和模型计算指出，任何一致的处理蛋白质中的静电相互作用应考虑以下几点。溶剂极化是计算两两静电相互作用的一个重要因素。溶剂极化实质上影响静电能和作用于电荷的力。有效介电常数Deff的简单表达式通常是无效的，因为Deff是位置的敏感函数。涉及偶极基团的成对相互作用的溶剂筛选不如变化的筛选有效。事实上，对于许多涉及偶极子的相互作用，溶剂屏蔽基本上可以忽略。电荷的自身能量对蛋白质的总静电能有很大的贡献。这必须通过与蛋白质中其他基团的特异性相互作用来补偿。将分析应用于已知结构的蛋白质的策略进行了讨论。
A classical treatment of electrostatic interactions in proteins is presented. The protein is treated as a region of low dielectric constant with spherical charges embedded within it, surrounded by an aqueous solvent of high dielectric constant, which may contain a simple electrolyte. The complete analysis includes the effects of solvent screening, polarization forces, and self energies, which are related to solvation energies. Formulae, and sample calculations of forces and energies, are given for the special case of a spherical protein. Our analysis and model calculations point out that any consistent treatment of electrostatic interactions in proteins should account for the following. Solvent polarization is an important factor in the calculation of pairwise electrostatic interactions. Solvent polarization substantially affects both electrostatic energies and forces acting upon charges. No simple expression for the effective dielectric constant, Deff, can generally be valid, since Deff is a sensitive function of position. Solvent screening of pairwise interactions involving dipolar groups is less effective than the screening of changes. In fact for many interactions involving dipoles, solvent screening can be essentially ignored. The self energy of charges makes a large contribution to the total electrostatic energy of a protein. This must be compensated by specific interactions with other groups in the protein. Strategies for applying the analysis to proteins whose structures are known are discussed.