...
首页> 外文期刊>Protein Engineering >A fast empirical approach to binding free energy calculations based on protein interface information.
【24h】

A fast empirical approach to binding free energy calculations based on protein interface information.

机译:一种快速的基于蛋白质界面信息的结合自由能计算的经验方法。

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       

摘要

Three useful variables from the interfaces of 20 protein-protein complexes were investigated. These variables are the side-chain accessible number (N(b)), the number of hydrophilic pairs (N(pair)) and buried apolar solventaccessible surface areas (DeltaDeltaASA(apol)). An empirical model based on the three variables was developed to describe the free energy of protein associations. As the results show, the side-chain accessible numbers characterize the loss of side-chain conformational entropy of protein interactions and the effective empirical function presented here has great capability for estimating the binding free energy. It was found that the variables of interface information capture most of the significant features of protein-protein association. Also, we applied the model based on the variables as a rescoring function to docking simulations and found that it has the potential to distinguish the 'true' binding mode. It is clear that the simple and empirical scale developed here is an attractive target function for calculating binding free energy for various biological processes to rational protein design.
机译:从20种蛋白质-蛋白质复合物的界面研究了三个有用的变量。这些变量是侧链可及数量(N(b)),亲水对的数量(N(pair))和埋藏的非极性溶剂可及的表面积(DeltaDeltaASA(apol))。建立了基于三个变量的经验模型来描述蛋白质缔合的自由能。结果表明,侧链可及数表征了蛋白质相互作用的侧链构象熵的损失,并且此处提供的有效经验功能具有很大的估计结合自由能的能力。发现界面信息的变量捕获了蛋白质-蛋白质缔合的大多数重要特征。同样,我们将基于变量的模型作为对账函数的对账函数应用于对接模拟,发现该模型具有区分“真实”绑定模式的潜力。显然,这里开发的简单和经验规模是一个吸引人的目标函数,用于计算各种生物学过程对合理蛋白质设计的结合自由能。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号