...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Analysis of the Structural and Dynamic Properties of Human N-Terminal Domain of Apolipoprotein E by Molecular Dynamics Simulations
【24h】

Analysis of the Structural and Dynamic Properties of Human N-Terminal Domain of Apolipoprotein E by Molecular Dynamics Simulations

机译：分子动力学模拟分析载脂蛋白E人N末端结构域的结构和动力学性质

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

Whereas the lipid-free N-terminal domain of apolipoprotein E (apoE-NT) adopts a four-helix bundle, the lipid-bound form is believed to undergo a large conformational change likely to be characterized by the opening of the bundle. ApoE-NT in a water/alcohol mixture was also shown to experience conformational changes exhibiting similarities with those induced upon lipid binding. The structure and dynamics of apoE-NT have been here investigated by analyzing 40 ns and 60 ns molecular dynamics simulations performed in water and in a water/propanol mixture, respectively. The overall structural properties show alterations of the tertiary structure of apoE-NT in the water/alcohol system in agreement with those observed experimentally. In contrast, in the water simulation, the sampled conformations remain closer to the crystal structure that served as a starting point for both simulations. Interestingly, several propanol molecules are seen to penetrate two hydrophobic regions of the bundle interior. One of these regions is enclosed in part by the short helix (H1') connecting helices 1 and 2 of the bundle which has been experimentally shown to be important for modulating lipid binding activity of apoE-NT. Principal component analysis of the water/propanol trajectory confirms that the region including H1' is the locus of the largest motion. Another region involves the loop connecting helix 2 and helix 3 which has been hypothesized to play the role of a hinge in the opening of the bundle.
机译：载脂蛋白E（apoE-NT）的无脂质N末端结构域采用四螺旋束，但脂质结合形式据信经历了很大的构象变化，其特征可能是束打开。还显示出水/醇混合物中的ApoE-NT经历构象变化，该构象变化与脂质结合诱导的构象变化相似。通过分析分别在水和水/丙醇混合物中进行的40 ns和60 ns分子动力学模拟，研究了apoE-NT的结构和动力学。总体结构性质表明，水/醇系统中apoE-NT的三级结构发生了变化，与实验观察到的一致。相反，在水模拟中，采样的构象保持更接近作为两种模拟起点的晶体结构。有趣的是，可以看到几个丙醇分子穿透了束内部的两个疏水区域。这些区域之一被连接束的螺旋1和2的短螺旋（H1'）部分包围，该螺旋已被实验证明对调节apoE-NT的脂质结合活性很重要。对水/丙醇轨迹的主成分分析证实，包括H1'的区域是最大运动的轨迹。另一个区域涉及连接螺旋线2和螺旋线3的环，已经假设其在束的开口中起到铰链的作用。

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