MOTIONAL MODES IN ACTIN MEASURED BY ANISOTROPY

这个项目将确定肌肉的运动模式 蛋白质肌动蛋白。这种蛋白质经历阳离子介导的聚合。 丝状肌动蛋白；正是这种形式与肌球蛋白偶联 产生肌肉力量。我们正在利用磷光各向异性来 测量分子和分子的大尺度运动模式 二价阳离子对F-肌动蛋白中这些运动的影响 (丝状)。我们将对其内在模式进行研究。 分子的运动和其他形式的内部和节段性 柔韧性及阳离子和ATP/ADP对这些运动的影响 (聚合是通过三磷酸腺苷的水解来调节的)以及这些运动是如何 丝状形态的变化。基本的想法是调查如何 运动方式对其生理功能起着一定的作用 (肌动球蛋白力的产生)以及单体的运动 成对/形成细丝运动的基础。为了做到这一点，我们 色氨酸各向异性测定方案的研究进展 采用时间相关的单光子计数方法。

This project will be to determine the motional modes of the muscle protein actin. This protein undergoes cation-mediated polymerization to filamentous actin; it is this form which couples with myosin to generate muscular force. We are using phosphorescence anisotropy to measure the large-scale modes of motion of the molecule and the influence of divalent cations on these motions in F-actin (filamentous). We will perform studies of the intrinsic modes of motion of the molecule and other forms of internal and segmental flexibility and the influence of cations and ATP/ADP on these motions (polymerization is mediated by ATP hydrolysis) and how these motions change in the filamentous form. The basic idea is to investigate how the modes of motion play a role in its physiological function (actomyosin force generation) and how the motion of the monomer couples/forms the basis for motion of the filament. To do this we plan on measuring tryptophan anisotropy in single trypto phan mutan ts using time correlated single photon counting methods.