首页> 外文期刊>Journal of Biological Physics >Temperature and solvent dependence of the dynamical landscape of tau protein conformations
【24h】

Temperature and solvent dependence of the dynamical landscape of tau protein conformations

机译:温度和溶剂依赖性的tau蛋白构象的动态格局

获取原文
获取原文并翻译 | 示例
           

摘要

We report the variation with temperature of the ensemble distribution of conformations spanned by the tau protein in its dynamical states measured by small-angle X-ray scattering (SAXS) using synchrotron radiation. The SAXS data show a clear temperature variation of the distribution of occupied protein conformations from 293 to 318 K. More conformations with a smaller radius of gyration are occupied at higher temperature. The protein–solvent interactions are shown by computer simulation to be essential for controlling the dynamics of protein conformations, providing evidence for the key role of water solvent in the protein dynamics, as proposed by Giorgio Careri.
机译:我们报告了tau蛋白跨越其动态状态的构象的总体分布的温度随温度的变化,该动态状态通过使用同步加速器辐射的小角X射线散射(SAXS)测量。 SAXS数据显示,从293到318 K的蛋白质占据的构象分布具有明显的温度变化。在较高的温度下,具有较小回转半径的更多构象被占据。通过计算机模拟显示,蛋白质与溶剂的相互作用对于控制蛋白质构象的动力学至关重要,这提供了证据,证明了水溶剂在蛋白质动力学中的关键作用,这一点由Giorgio Careri提出。

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