...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Shifting hydrogen bonds may produce flexible transmembrane helices
【24h】

Shifting hydrogen bonds may produce flexible transmembrane helices

机译：氢键移位可能会产生柔性跨膜螺旋

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 intricate functions of membrane proteins would not be possible without bends or breaks that are remarkably common in trans-membrane helices. The frequent helix distortions are nevertheless surprising because backbone hydrogen bonds should be strong in an apolar membrane, potentially rigidifying helices. It is therefore mysterious how distortions can be generated by the evolutionary currency of random point mutations. Here we show that we can engineer a transition between distinct distorted helix conformations in bacteriorhodopsin with a single-point mutation. Moreover, we estimate the energetic cost of the conformational transitions to be smaller than 1 kcal/mol. We propose that the low energy of distortion is explained in part by the shifting of backbone hydrogen bonding partners. Consistent with this view, extensive backbone hydrogen bond shifts occur during helix conformational changes that accompany functional cycles. Our results explain how evolution has been able to liberally exploit transmembrane helix bending for the optimization of membrane protein structure, function, and dynamics.
机译：如果没有跨膜螺旋中常见的弯曲或断裂，膜蛋白的复杂功能将无法实现。但是，频繁的螺旋变形令人惊讶，因为主链氢键在非极性膜中应该很牢固，从而可能使螺旋硬化。因此，神秘的是如何通过随机点突变的进化货币产生扭曲的。在这里，我们表明我们可以通过单点突变设计细菌视紫红质中不同的扭曲螺旋构象之间的过渡。此外，我们估计构象转变的能量成本小于1 kcal / mol。我们提出，低变形能的部分原因是主链氢键伙伴的移动。与该观点一致的是，在伴随功能循环的螺旋构象变化期间发生大量的主链氢键移位。我们的结果解释了进化是如何能够自由地利用跨膜螺旋弯曲来优化膜蛋白结构，功能和动力学的。

著录项

  • 来源
  • 作者

    Zheng Cao; James U. Bowie;

  • 作者单位

    Department of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, Molecular Biology Institute, University of California,Bover Hall. 611 Charles E. Youna Drive East. Los Anaeles. CA 90095;

    Department of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, Molecular Biology Institute, University of California,Bover Hall. 611 Charles E. Youna Drive East. Los Anaeles. CA 90095;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    kinks; proline; protein dynamics; protein folding;

    机译：扭结脯氨酸蛋白质动力学蛋白质折叠;

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