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胱氨酸塞和其他二聚体蛋白质中具有大机械稳定性的新型机制。

Cystine plug and other novel mechanisms of large mechanical stability in dimeric proteins.

机构信息

Institute of Physics, Polish Academy of Sciences, Al. Lotników 32/46, 02-668 Warsaw, Poland.

出版信息

Phys Rev Lett. 2012 Nov 16;109(20):208101. doi: 10.1103/PhysRevLett.109.208101. Epub 2012 Nov 13.

Abstract

We identify three dimeric proteins whose mechanostability is anisotropic and should exceed 1 nN along some directions. They come with distinct mechanical clamps: either shear-based, or involving a cystine slipknot, or due to dragging of a cystine plug through a cystine ring. The latter two mechanisms are topological in nature; the cystine plug mechanism has not yet been discussed but it turns out to provide the largest resistance to stretching. Its possible applications in elastomers are discussed.

摘要

我们鉴定出三种二聚体蛋白,其力学稳定性具有各向异性,在某些方向上应超过 1 nN。它们带有独特的机械夹具:要么是基于剪切的,要么涉及半胱氨酸滑结,要么是由于半胱氨酸塞通过半胱氨酸环的拖拽。后两种机制在本质上是拓扑的;虽然尚未讨论半胱氨酸塞机制,但事实证明它能提供最大的抗拉伸阻力。讨论了其在弹性体中的可能应用。

相似文献

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Formation of cystine slipknots in dimeric proteins.二聚体蛋白质中胱氨酸滑环的形成。
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Topological features in stretching of proteins.蛋白质拉伸中的拓扑特征。
Biochem Soc Trans. 2013 Apr;41(2):519-22. doi: 10.1042/BST20120289.

引用本文的文献

1
Formation of cystine slipknots in dimeric proteins.二聚体蛋白质中胱氨酸滑环的形成。
PLoS One. 2013;8(3):e57443. doi: 10.1371/journal.pone.0057443. Epub 2013 Mar 8.

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