Institute of Mechanics, Lomonosov Moscow State University, Moscow, Russia.
Biochemistry (Mosc). 2011 Dec;76(13):1484-506. doi: 10.1134/S0006297911130086.
The interaction of actin and myosin powers striated and smooth muscles and some other types of cell motility. Due to its highly ordered structure, skeletal muscle is a very convenient object for studying the general mechanism of the actin-myosin molecular motor. The history of investigation of the actin-myosin motor is briefly described. Modern concepts and data obtained with different techniques including protein crystallography, electron microscopy, biochemistry, and protein engineering are reviewed. Particular attention is given to X-ray diffraction studies of intact muscles and single muscle fibers with permeabilized membrane as they give insight into structural changes that underlie force generation and work production by the motor. Time-resolved low-angle X-ray diffraction on contracting muscle fibers using modern synchrotron radiation sources is used to follow movement of myosin heads with unique time and spatial resolution under near physiological conditions.
肌动蛋白和肌球蛋白的相互作用为有条纹和无条纹肌肉以及其他一些类型的细胞运动提供动力。由于其高度有序的结构，骨骼肌是研究肌动球蛋白分子马达一般机制的非常方便的对象。简要描述了肌球蛋白马达的研究历史。回顾了包括蛋白质晶体学、电子显微镜、生物化学和蛋白质工程在内的不同技术获得的现代概念和数据。特别关注用通透膜处理的完整肌肉和单根肌纤维的 X 射线衍射研究，因为它们深入了解了力产生和马达做功的结构变化。使用现代同步辐射源对收缩肌纤维进行的时间分辨低角度 X 射线衍射，可在近生理条件下以独特的时间和空间分辨率跟踪肌球蛋白头部的运动。
