...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Non-Crystalline Solids: A Journal Devoted to Oxide, Halide, Chalcogenide and Metallic Glasses, Amorphous Semiconductors, Non-Crystalline Films, Glass-Ceramics and Glassy Composites >Is the rigid-body assumption reasonable?: Insights into the effects of dynamics on the electrostatic analysis of barnase-barstar
【24h】

Is the rigid-body assumption reasonable?: Insights into the effects of dynamics on the electrostatic analysis of barnase-barstar

机译：刚体假设是否合理？：洞察动力学对barnase-barstar静电分析的影响

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Electrostatically-driven association of proteins is important to many biological functions, and understanding which amino acid residues contribute to these interactions is crucial to protein design. Theoretical calculations that are used to elucidate the role of electrostatics in association are typically based on a single experimentally determined protein structure, while an underlying rigid-body assumption is adopted. The goal of this study was to investigate the role of conformational fluctuations on electrostatic interaction energies, as applied to the electrostatic analysis of barnase-barstar. For our calculations, we apply theoretical alanine-scan mutagenesis to introduce charge perturbations by replacing every ionizable residue with alanine, one at a time. Electrostatic clustering and free energy calculations based on the Poisson-Boltzmann method are used to evaluate the effects of each perturbation. Molecular dynamics simulations are performed for the barnase-barstar parent complex and seven experimental alanine mutations from the literature, in order to introduce relaxation before and after mutation. We discuss the effects of dynamics, in the form of pre- and post-mutation relaxation, on electrostatic clustering and free energies of association in light of experimental data. We also examine the utility of nine electrostatic similarity methods for clustering of barnase alanine-scan mutants. Our calculations suggest that the rigid-body assumption is reasonable for electrostatic calculations of barnase-barstar.
机译：蛋白质的静电驱动缔合对许多生物学功能很重要，了解哪些氨基酸残基有助于这些相互作用对蛋白质设计至关重要。用于阐明静电作用的理论计算通常基于单个实验确定的蛋白质结构，而采用了基本的刚性假设。这项研究的目的是研究构象波动对静电相互作用能的作用，并将其应用于barnase-barstar的静电分析。对于我们的计算，我们应用理论上的丙氨酸扫描诱变技术，通过每次用丙氨酸替换每个可电离的残基来引入电荷扰动。基于Poisson-Boltzmann方法的静电聚类和自由能计算用于评估每个扰动的影响。分子动力学模拟对barnase-barstar母体复合物和文献中的七个实验性丙氨酸突变进行了研究，目的是在突变前后引入松弛。根据实验数据，我们讨论了突变前和突变后形式的动力学对静电聚集和缔合自由能的影响。我们还检查了9种静电相似性方法对barnase丙氨酸扫描突变体的聚类的实用性。我们的计算表明，刚体假设对于barnase-barstar的静电计算是合理的。

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