Muscular force is the sum of unitary force interactions generated as filaments of myosins move forcibly along parallel filaments of actins, understanding that the free energy required comes from myosin-catalyzed ATP hydrolysis. Using results from conventional biochemistry, our own mutational studies, and diffraction images from others, we attempt, in molecular detail, an account of a unitary interaction, i.e., what happens after a traveling myosin head, bearing an ADP-P(i), reaches the next station of an actin filament in its path. We first construct a reasonable model of the myosin head and actin regions that meet to form the "weakly bound state". Separately, we consider Holmes' model of the rigor state [Holmes, K. C., Angert, I., Kull, F. J., Jahn, W. & Schröder, R. R. (2003) Nature 425, 423-427], supplemented with several heretofore missing residues, thus realizing the "strongly bound state." Comparing states suggests how influences initiated at the interface travel elsewhere in myosin to discharge various functions, including striking the actins. Overall, state change seems to occur by attachment of a hydrophobic triplet (Trp-546, Phe-547, and Pro-548) of myosin to an actin conduit with a hydrophobic guiding rail (Ile-341, Ile-345, Leu-349, and Phe-352) and the subsequent linear movement of the triplet along the rail.

译文

:肌力是肌球蛋白丝沿着平行的肌动蛋白丝强行运动时产生的单位力相互作用的总和,要了解所需的自由能来自肌球蛋白催化的ATP水解。利用常规生物化学的结果,我们自己的突变研究以及其他研究的衍射图像,我们尝试在分子细节上解释整体相互作用,即,在移动的肌球蛋白头部携带ADP-P(i)后发生的情况,到达其路径中肌动蛋白丝的下一个位置。我们首先构建一个肌球蛋白头部和肌动蛋白区域的合理模型,这些区域相遇形成“弱结合状态”。单独地,我们考虑严格状态的福尔摩斯模型[Holmes,KC,Angert,I.,Kull,FJ,Jahn,W.&Schröder,RR(2003)Nature 425,423-427],并补充了一些迄今为止遗漏的残基,从而实现“强绑定状态”。比较状态表明在界面处引发的影响如何在肌球蛋白中传播到其他位置,以发挥各种功能,包括打击肌动蛋白。总体而言,状态变化似乎是通过将肌球蛋白的疏水三联体(Trp-546,Phe-547和Pro-548)连接到带有疏水导轨(Ile-341,Ile-345,Leu-349)的肌动蛋白导管而发生的。 ,以及Phe-352)以及随后的三重态沿轨道的线性运动。

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