Anisotropic Contributions to Protein-Protein Interactions.
Anisotropic Contributions to Protein-Protein Interactions.
复制标题
蛋白质-蛋白质相互作用的各向异性贡献。
DOI：
10.1021/ct4006695
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发表时间：
2014
影响因子：
5.5
通讯作者：
A. Lenhoff
中科院分区：
文献类型：
--
作者：
L. Quang;S. Sandler;A. Lenhoff
蛋白质的形状和功能的各向异性使蛋白质-蛋白质相互作用的预测变得复杂。我们研究了两个球状蛋白质，溶菌酶和凝乳酶B，这两个球状蛋白质的分子量相差约2倍，这些相互作用的静电和非静电贡献的分布。这些蛋白质的相互作用趋势计算的渗透第二维里系数，使用原子模型的蛋白质进行评估的贡献。我们的重点是确定的取向配置，有助于最强烈的整体相互作用，由于高互补性的相互作用，并计算离子强度对这种相互作用的影响。结果强调了蛋白质相互作用的几个特征的定量重要性，特别是，尽管它们的发生频率不同，但相互作用能明显不同的配置可以对整体相互作用做出有意义的贡献。然而，相对较小的影响，由于电荷各向异性或特定的水合作用可以影响整体的相互作用显着，只有当它们有助于强烈吸引力的配置。结果强调，详细的各向异性，以捕捉实际的实验趋势，甚至非常详细的原子模型的敏感性微妙的解决方案的贡献占的必要性。
The anisotropy of shape and functionality of proteins complicates the prediction of protein-protein interactions. We examine the distribution of electrostatic and nonelectrostatic contributions to these interactions for two globular proteins, lysozyme and chymosin B, which differ in molecular weight by about a factor of 2. The interaction trends for these proteins are computed in terms of contributions to the osmotic second virial coefficient that are evaluated using atomistic models of the proteins. Our emphasis is on identifying the orientational configurations that contribute most strongly to the overall interactions due to high-complementarity interactions, and on calculating the effect of ionic strength on such interactions. The results emphasize the quantitative importance of several features of protein interactions, notably that despite differences in their frequency of occurrence, configurations differing appreciably in interaction energy can contribute meaningfully to overall interactions. However, relatively small effects due to charge anisotropy or specific hydration can affect the overall interaction significantly only if they contribute to strongly attractive configurations. The results emphasize the necessity of accounting for detailed anisotropy to capture actual experimental trends, and the sensitivity of even very detailed atomistic models to subtle solution contributions.
DOI：
10.1073/pnas.84.20.7079
发表时间：
1987-10
影响因子：
11.1
作者：
J. Thomson;P. Schurtenberger;G. Thurston;G. Benedek
通讯作者：
J. Thomson;P. Schurtenberger;G. Thurston;G. Benedek
DOI：
10.1073/pnas.89.4.1214
发表时间：
1992-02-15
影响因子：
11.1
作者：
BERLAND, CR;THURSTON, GM;BENEDEK, GB
通讯作者：
BENEDEK, GB
DOI：
10.1073/pnas.88.13.5660
发表时间：
1991-07-01
影响因子：
11.1
作者：
BROIDE, ML;BERLAND, CR;BENEDEK, GB
通讯作者：
BENEDEK, GB