关于肌肉中化学机械能转换的分子基础。
On the molecular basis for chemomechanical energy transduction in muscle.
作者信息
Morales M F, Botts J
出版信息
Proc Natl Acad Sci U S A. 1979 Aug;76(8):3857-9. doi: 10.1073/pnas.76.8.3857.
Abstract
Herein it is developed that energy transduction in muscle is an activity of myosin S-1 and its ligands, actin (A) and nucleotide (N). S-1 shares with other molecular particles (e.g., hemoglobin) the property that binding events at one of its sites, the N-site, influences binding events at a remote site, the A site (specifically, influences both the actin affinity and actin attachment angle at the A site). However, there is a crucial difference between S-1 and the better-known systems. Because the N site is enzymatic, it has a temporal sequence of occupants; this imposes a temporal sequence of actin attitudes--i.e., a sequence of mechanical events.
摘要
在此揭示，肌肉中的能量转导是肌球蛋白S-1及其配体肌动蛋白（A）和核苷酸（N）的一种活动。S-1与其他分子颗粒（如血红蛋白）具有共同特性，即其一个位点（N位点）的结合事件会影响远处另一个位点（A位点）的结合事件（具体而言，会影响A位点处的肌动蛋白亲和力和肌动蛋白附着角度）。然而，S-1与更知名的系统之间存在一个关键差异。由于N位点具有酶活性，其占据者有一个时间顺序；这就强加了肌动蛋白姿态的时间顺序——即一系列机械事件。
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