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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Probes bound to myosin Cys-707 rotate during length transients in contraction
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Probes bound to myosin Cys-707 rotate during length transients in contraction

机译：与肌球蛋白Cys-707结合的探针在收缩的长度瞬变过程中旋转

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摘要

It is widely conjectured that muscle shortens because portions of myosin molecules (the "cross-bridges") impel the actin filament to which they transiently attach and that the impulses result from rotation of the cross-bridges. Crystallography indicates that a cross-bridge is articulated- consisting of a globular catalytic/actin-binding domain and a long lever arm that may rotate. Conveniently, a rhodamine probe with detectable attitude can be attached between the globular domain and the lever arm, enabling the observer to tell whether the anchoring region rotates. Well-established signature effects observed in shortening are tension changes resulting from the sudden release or quick stretch of active muscle fibers. In this investigation we found that closely correlated with such tension changes are changes in the attitude of the rhodamine probes. This correlation strongly supports the conjecture about how shortening is achieved.
机译：人们普遍认为，肌肉缩短是因为肌球蛋白分子的一部分（“跨桥”）推动了肌动蛋白丝，而肌动蛋白丝暂时连接在肌动蛋白丝上，并且冲动是由跨桥的旋转引起的。晶体学研究表明，一个跨接桥由球形的催化/肌动蛋白结合域和一个可以旋转的长杠杆臂组成。可以方便地在球状区域和杠杆臂之间连接可检测姿势的若丹明探针，使观察者能够分辨出锚定区域是否旋转。在起酥油中观察到的公认的特征效应是由于活性肌纤维突然释放或快速拉伸而引起的张力变化。在这项调查中，我们发现与这种张力变化密切相关的是若丹明探针的姿态变化。这种相关性强烈支持关于如何实现缩短的推测。

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