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Rough passage across a barrier

机译:穿越障碍物的艰难通道

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摘要

Proteins fluctuate between different conformations to perform their sophisticated tasks. The random motion of water molecules around proteins provides an inexhaustible reservoir of thermal 'kicks', which act as the molecular driving forces of such conformational dynamics. Counterintuitively, the same thermal motions of the solvent also limit the speed of biomolecular motion, an effect known as solvent friction. But it has become increasingly clear that, in some important cases, friction within a protein molecule might be the dominant impediment to its molecular dynamics. In this issue, Chung and Eaton1 (page 685) report one of the most impressive studies so far in which the contribution of such internal friction to dynamics is quantified for protein molecules caught in the act of folding. Remarkably, the results have implications far beyond protein folding.
机译:蛋白质在不同的构象之间波动以执行其复杂的任务。水分子围绕蛋白质的随机运动提供了不竭的热“壁垒”,这些壁垒是这种构象动力学的分子驱动力。与直觉相反,溶剂的相同热运动也限制了生物分子运动的速度,这种作用称为溶剂摩擦。但是,越来越明显的是,在某些重要情况下,蛋白质分子内的摩擦可能是其分子动力学的主要障碍。在本期中,Chung和Eaton1(第685页)报告了迄今为止最令人印象深刻的研究之一,其中定量分析了折叠行为中捕获的蛋白质分子的内摩擦对动力学的贡献。值得注意的是,结果的意义远不止蛋白质折叠。

著录项

  • 来源
    《Nature》 |2013年第7473期|632-633|共2页
  • 作者

    BENJAMIN SCHULER; JANE CLARKE;

  • 作者单位

    Department of Biochemistry, University of Zurich. 8057 Zurich, Switzerland;

    Wellcome Trust Senior Research Fellow in the Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);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
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