...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Macromolecular theory and simulations >Folding of polyalanine into helical hairpins
【24h】

Folding of polyalanine into helical hairpins

机译：将聚丙氨酸折叠成螺旋发夹

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

The variation of the secondary structure and dimensions of long PA peptides was examined by means of all-atom MD simulations. It was found that on cooling, instead of straight helices, hairpin-like structures with two and three parallel helical legs were formed. The exclusive population of hairpins in PA at room temperature was proved by the bimodality of the distribution functions of the end-to-end distance and the radius of gyration. The helix-turn-helix motif revealed in PA simulations is pertinent for the structure of transmembrane proteins. The potential energy analysis showed a crucial role of the van der Waals forces in stabilization of the hairpins. It was underlined that this is a feature shared with folding of hydrocarbon chains, such as PE, into the crystal lamellae. In long polyalanine molecules in non-polar medium at ambient temperature the straight alpha-helix is replaced by the hairpin structures with two or three helical legs. The striking bimodality of the distribution functions of the end-to-end distance P(R) proves exclusive population of hairpins. The packing of α-helices in the parallel position in hairpins is stabilized by van der Waals interaction.
机译：通过全原子MD模拟检查了长PA肽的二级结构和尺寸的变化。发现在冷却时，代替了直螺旋，形成了具有两个和三个平行的螺旋腿的发夹状结构。室温下PA中发夹的唯一种群由端对端距离和回转半径的分布函数的双峰性证明。 PA模拟中揭示的螺旋-转-螺旋基序与跨膜蛋白的结构有关。势能分析表明范德华力在稳定发夹中起着至关重要的作用。强调指出，这是烃链（例如PE）折叠成晶体薄片所共有的特征。在室温下在非极性介质中的长聚丙氨酸分子中，直的α-螺旋被具有两个或三个螺旋腿的发夹结构取代。端到端距离P（R）的分布函数具有惊人的双峰性，证明了发夹的排他性。发夹中平行位置的α螺旋堆积通过范德华相互作用得以稳定。

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