MOTIONAL MODES IN ACTIN MEASURED BY ANISOTROPY

这个项目正在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)。我有兴趣做一些内在的研究。 分子的运动方式和其他形式的内部和 节段柔韧性及阳离子和ATP/ADP对其影响 这些运动(聚合是通过三磷酸腺苷的水解来调节的)以及如何 这些运动以丝状形式变化。基本的想法是 研究运动模式如何在其生理功能中发挥作用 功能(肌动球蛋白力的产生)和如何运动 单体偶联/形成细丝运动的基础。去做 我们计划测量单个W突变体的色氨酸各向异性。

This project is determining 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). I am interested in doing some 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 W mutants.