首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >From the Cover: The titin-telethonin complex is a directed superstable molecular bond in the muscle Z-disk
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From the Cover: The titin-telethonin complex is a directed superstable molecular bond in the muscle Z-disk

机译:从封面开始:titin-telethonin复合物是肌肉Z盘中的定向超稳定分子键

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摘要

Mechanical stability of bonds and protein interactions has recently become accessible through single molecule mechanical experiments. So far, mechanical information about molecular bond mechanics has been largely limited to a single direction of force application. However, mechanical force acts as a vector in space and hence mechanical stability should depend on the direction of force application. In skeletal muscle, the giant protein titin is anchored in the Z-disk by telethonin. Much of the structural integrity of the Z-disk hinges upon the titin-telethonin bond. In this paper we show that the complex between the muscle proteins titin and telethonin forms a highly directed molecular bond. It is designed to resist ultra-high forces if they are applied in the direction along which it is loaded under physiological conditions, while it breaks easily along other directions. Highly directed molecular bonds match in an ideal way the requirements of tissues subject to mechanical stress.
机译:键和蛋白质相互作用的机械稳定性最近已通过单分子机械实验获得。到目前为止,有关分子键合力学的机械信息在很大程度上已限于单一作用力方向。但是,机械力在空间中充当矢量,因此机械稳定性应取决于施加力的方向。在骨骼肌中,巨大的蛋白滴定蛋白被Telethonin锚定在Z盘中。 Z盘的大部分结构完整性都取决于titin-telethonin键。在本文中,我们表明肌肉蛋白titin和Telethonin之间的复合物形成了高度定向的分子键。如果在生理条件下按施加的方向施加超高力,则它可以抵抗超高的力,而在其他方向上则容易断裂。高度定向的分子键以理想的方式匹配经受机械应力的组织的要求。

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