Partial molar volume of proteins studied by the three-dimensional reference interaction site model theory
Partial molar volume of proteins studied by the three-dimensional reference interaction site model theory
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DOI：
10.1021/jp045667c
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发表时间：
2005-04-14
影响因子：
3.3
通讯作者：
Hirata, F
中科院分区：
文献类型：
--
作者：
Imai, T;Kovalenko, A;Hirata, F
三维参考相互作用位点模型（3D-RISM）理论应用于分析水合对蛋白质偏摩尔体积的影响。对于一些蛋白质的天然结构，利用3D-RISM理论结合几何体积计算将偏摩尔体积分解为几何贡献和水合贡献。水合作用与蛋白质的表面特性相关。热体积是由水分子的热波动引起的蛋白质周围空隙的体积，与蛋白质可到达的表面积成正比。相互作用体积是蛋白质和水分子之间静电相互作用的贡献，显然由蛋白质表面上的带电原子团控制。极性原子团对相互作用体积没有任何贡献。本方法还分析了溶菌酶低压和高压结构之间的体积差异。
The three-dimensional reference interaction site model (3D-RISM) theory is applied to the analysis of hydration effects on the partial molar volume of proteins. For the native structure of some proteins, the partial molar volume is decomposed into geometric and hydration contributions using the 3D-RISM theory combined with the geometric volume calculation. The hydration contributions are correlated with the surface properties of the protein. The thermal volume, which is the volume of voids around the protein induced by the thermal fluctuation of water molecules, is directly proportional to the accessible surface area of the protein. The interaction volume, which is the contribution of electrostatic interactions between the protein and water molecules, is apparently governed by the charged atomic groups on the protein surface. The polar atomic groups do not make any contribution to the interaction volume. The volume differences between low- and high-pressure structures of lysozyme are also analyzed by the present method.