Walker M, Trinick J, White H
Muscle and Collagen Group, Bristol University Veterinary School, Langford, United Kingdom.
Biophys J. 1995 Apr;68(4 Suppl):87S-91S.
The structure of the AM-ATP transient kinetic state of the acto-myosin ATPase cycle has been examined by electron microscopy using frozen-hydrated specimens prepared in low ionic strength. By spraying grids layered with the acto-S1 complex with ATP immediately before freezing, it was possible to examine the structure of the ternary complex with a time resolution of 10 ms. Disordered binding of the S1 was observed, suggesting more than one attachment geometry. This could be due to the presence of more than one biochemical intermediate, or to a single intermediate binding in more than one conformation.
利用在低离子强度下制备的冷冻水合标本，通过电子显微镜研究了肌动蛋白-肌球蛋白ATP酶循环中AM-ATP瞬态动力学状态的结构。通过在冷冻前立即用ATP喷射铺有肌动蛋白-S1复合物的网格，能够以10毫秒的时间分辨率研究三元复合物的结构。观察到S1的无序结合，这表明存在不止一种附着几何结构。这可能是由于存在不止一种生化中间体，或者是由于单一中间体以不止一种构象结合。
