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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A new direction for titin pulling
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A new direction for titin pulling

机译：提力素的新方向

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摘要

Many proteins are known to serve roles as structural scaffolds in cells and tissues. These proteins maintain the shape of the cell, act as local force sensors, and are essential to form tissues that are exposed to large external forces. Although seemingly passive elements, these structural proteins have unique physical features that are worthy of a closer look. In particular, it is critically important to understand how scaffolding proteins and protein complexes respond to the high external forces commonly encoun'ered in biology. In this issue of PNAS, Bertz et al. (1) report a remarkable rev, feature of these load-bearing complexes. Apparently, evolution has molded these proteins to be remarkably resistant to unfolding when pulled in the same direction as they would experience in the cell. However, in other pulling directions the complex is relatively fragile.
机译：已知许多蛋白质在细胞和组织中充当结构支架。这些蛋白质维持细胞的形状，充当局部力传感器，并且对于形成暴露于较大外力的组织是必不可少的。尽管这些结构蛋白看似是被动元件，但它们具有独特的物理特征，值得仔细研究。尤其重要的是，了解支架蛋白和蛋白复合物如何响应生物学中常见的高外力是至关重要的。在本期PNAS中，Bertz等人。 （1）报告了这些承重复合体的显着特征。显然，进化使这些蛋白质以与在细胞中经历的方向相同的方向被拉动时，具有显着的抗折叠能力。但是，在其他拉动方向，复合物相对脆弱。

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