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Hydrophobic interactions in context

机译：在上下文中的疏水相互作用

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Oil and water do not mix. At the molecular level, this 'de-mixing' tendency, known as the hydrophobic interaction, is thought to drive many self-assembly processes, such as protein folding, formation of micelles and membranes, and molecular recognition. On page 347 of this issue, Ma et al. present experimental evidence that the strength of hydrophobic interactions is dramatically affected by two biologically relevant cations - ammonium and guanidin-ium - when these ions are immobilized near hydrophobic patches of molecules. The oily core of a globular protein is formed by segregation of its hydrophobic groups. By contrast, protein surfaces are mosaics containing not only polar and charged groups, but also hydrophobic ones, which frequently occur in patches that are crucial for binding and recognizing other molecules, and for assembling proteins into larger structures. These patches do not exist in isolation, but reside in the chemical and topographical context of their surroundings. There is a growing realization from simulation studies that the surrounding chemical environment affects hydrophobic interactions in non-intuitive ways, but quantifying this effect experimentally has remained a challenge.
机译：油和水不混合。在分子水平上，这种“混合”趋势（称为疏水相互作用）被认为会驱动许多自组装过程，例如蛋白质折叠，胶束和膜的形成以及分子识别。在第347页上，Ma等人。目前的实验证据表明，当两种离子固定在分子的疏水斑点附近时，疏水相互作用的强度会受到两种生物学上相关的阳离子-铵和胍盐-的显着影响。球形蛋白的油性核心是通过其疏水基团的分离形成的。相比之下，蛋白质表面是不仅包含极性基团和带电基团，而且还包含疏水基团的镶嵌体，这些镶嵌体通常出现在对于结合和识别其他分子以及将蛋白质组装成更大结构至关重要的补丁中。这些斑块并不是孤立存在的，而是存在于周围环境的化学和地形环境中。通过仿真研究，人们逐渐意识到周围的化学环境以非直观的方式影响疏水相互作用，但是通过实验量化这种作用仍然是一个挑战。

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  • 来源
    《Nature》 |2015年第7534期|277-279|共3页
  • 作者

    SHEKHAR GARDE;

  • 作者单位

    Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York 12180, USA;

  • 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);
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