García de la Torre J, Bloomfield V A
Biochemistry. 1980 Oct 28;19(22):5118-23. doi: 10.1021/bi00563a028.
On the basis of the current knowledge of the structure and dimensions of myosin and its parts, we analyze available data on hydrodynamic properties (translational diffusion, rotational diffusion, and intrinsic viscosity) for comparison with values calculated for models with varying geometry. Special attention is paid to detecting flexibility effects in those properties. After obtaining a plausible model for subfragment S-1, we concentrate on the conformation of the rodlike parts of myosin. Although uncertainties in the experimental values do not allow a rigorous, quantitative analysis, we show how hydrodynamic data provide evidence for the flexibility of the rod at the joint of subfragment S-2 and light meromyosin.
基于目前对肌球蛋白及其各部分结构和尺寸的了解，我们分析了有关流体动力学性质（平动扩散、转动扩散和特性粘度）的现有数据，以便与针对具有不同几何形状的模型计算出的值进行比较。特别关注检测这些性质中的柔性效应。在获得一个合理的亚片段S-1模型后，我们将重点放在肌球蛋白杆状部分的构象上。尽管实验值的不确定性不允许进行严格的定量分析，但我们展示了流体动力学数据如何为亚片段S-2与轻酶解肌球蛋白连接处杆的柔性提供证据。
