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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Why Hofmeister effects of many salts favor protein folding but not DNA helix formation
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Why Hofmeister effects of many salts favor protein folding but not DNA helix formation

机译：为什么许多盐的霍夫迈斯特效应有利于蛋白质折叠而不是DNA螺旋形成

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摘要

The majority (～70%) of surface buried in protein folding is hydrocarbon, whereas in DNA helix formation, the majority (～65%) of surface buried is relatively polar nitrogen and oxygen. Our previous quantification of salt exclusion from hydrocarbon (C) accessible surface area (ASA) and accumulation at amide nitrogen (N) and oxygen (O) ASA leads to a prediction of very different Hofmeister effects on processes that bury mostly polar (N, O) surface compared to the range of effects commonly observed for processes that bury mainly nonpolar (C) surface, e.g., micelle formation and protein folding. Here we quantify the effects of salts on folding of the monomeric DNA binding domain (DBD) of lac repressor (lac DBD) and on formation of an oligomeric DNA duplex. In accord with this prediction, no salt investigated has a stabilizing Hofmeister effect on DNA helix formation. Our /ISA-based analyses of model compound data and estimates of the surface area buried in protein folding and DNA helix formation allow us to predict Hofmeister effects on these processes. We observe semiquantitative to quantitative agreement between these predictions and the experimental values, obtained from a novel separation of coulombic and Hofmeister effects. Possible explanations of deviations, including salt-dependent unfolded ensembles and interactions with other types of surface, are discussed.
机译：蛋白质折叠中埋藏的大部分表面（〜70％）是碳氢化合物，而在DNA螺旋形成过程中，埋藏的大部分表面（〜65％）是相对极性的氮和氧。我们先前对碳氢化合物（C）可及表面积（ASA）以及在酰胺氮（N）和氧（O）ASA处聚集的盐排阻进行定量分析得出的预测是，霍夫迈斯特对掩埋大部分极性（N，O与通常掩埋非极性（C）表面的过程通常观察到的作用范围相比，例如胶束形成和蛋白质折叠。在这里，我们量化了盐对lac阻遏物（lac DBD）的单体DNA结合域（DBD）折叠以及寡聚DNA双链体形成的影响。与该预测一致，没有研究的盐对DNA螺旋的形成具有稳定的霍夫迈斯特效应。我们基于/ ISA的模型化合物数据分析以及对蛋白质折叠和DNA螺旋形成中埋藏的表面积的估计，使我们能够预测霍夫迈斯特对这些过程的影响。我们观察到这些预测与实验值之间的半定量到定量一致性，这些结果是从库仑效应和霍夫迈斯特效应的新型分离中获得的。讨论了偏差的可能解释，包括与盐相关的未折叠集合以及与其他类型表面的相互作用。

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    Laurel M. Pegram; Timothy Wendorff; Robert Erdmann; Irina Shkel; Dana Bellissimo; Daniel J. Felitsky; M. Thomas Record Jr.;

  • 作者单位

    Departments of Biochemistry University of Wisconsin-Madison, Madison, WI 53706 Chemistry, University of Wisconsin-Madison, Madison, WI 53706;

    rnDepartments of Biochemistry University of Wisconsin-Madison, Madison, WI 53706;

    rnDepartments of Biochemistry University of Wisconsin-Madison, Madison, WI 53706 Department of Biology, Massachusetts Institute of Technology, Cam-bridge, MA 02139;

    rnDepartments of Biochemistry University of Wisconsin-Madison, Madison, WI 53706;

    rnDepartments of Biochemistry University of Wisconsin-Madison, Madison, WI 53706;

    rnDepartments of Biochemistry University of Wisconsin-Madison, Madison, WI 53706 Computational and Structural Chemistry, GlaxoSmithKline, Collegeville, PA 19426;

    rnDepartments of Biochemistry University of Wisconsin-Madison, Madison, WI 53706 Chemistry, University of Wisconsin-Madison, Madison, WI 53706;

  • 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

    Hofmeister salts; m-values; thermodynamics;

    机译：霍夫迈斯特盐;m值;热力学;

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