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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The coiled-coil of the human Rad50 DNA repair protein contains specific segments of increased flexibility
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The coiled-coil of the human Rad50 DNA repair protein contains specific segments of increased flexibility

机译：人类Rad50 DNA修复蛋白的卷曲螺旋包含增加柔性的特定片段

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摘要

Protein structural features are usually determined by defining regularities in a large population of homogeneous molecules. However, irregular features such as structural variation and flexibility are likely to be missed, despite their vital role for their biological function. In this paper, we report the observation of striking irregularities in the flexibility of the coiled-coil region of the human Rad50 DNA repair protein. Existing methods to quantitatively analyze flexibility are applicable to homogeneous polymers only. Because protein coiled-coils cannot be assumed to be homogeneous, we develop a method to quantify the local flexibility from high-resolution atomic force microscopy images. Indeed, in Rad50 coiled-coils, two positions of increased flexibility are observed. We discuss how this dynamic structural feature is integral to Rad50 function. [References: 20]
机译：蛋白质结构特征通常是通过在大量同质分子中定义规则性来确定的。然而，尽管不规则特征（如结构变异和柔韧性）对其生物学功能起着至关重要的作用，但仍可能会被遗漏。在本文中，我们报告了人类Rad50 DNA修复蛋白的卷曲螺旋区域的柔性中存在明显的不规则现象。定量分析柔韧性的现有方法仅适用于均相聚合物。因为不能认为蛋白质卷曲螺旋是同质的，所以我们开发了一种方法，可以从高分辨率原子力显微镜图像定量量化局部柔性。实际上，在Rad50盘绕线圈中，观察到两个位置的柔韧性都得到了提高。我们将讨论此动态结构特征如何与Rad50功能集成在一起。 [参考：20]

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