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Polymerization of actin filaments coupled with adenosine triphosphate hydrolysis: Brownian dynamics and theoretical analysis

机译:肌动蛋白丝的聚合加上三磷酸腺苷水解:布朗动力学和理论分析

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Polymerization dynamics of single actin filaments coupled with adenosine triphosphate (ATP) hydrolysis is investigated via both theoretical analysis and Brownian dynamics simulations. Brownian dynamics simulations have been applied recently to study the growth behaviors of long filaments as a function of the free actin monomer concentrations, C_T, which is found to be in agreement with the associated experiments. In the present study, both ATP cap length and length diffusivity are studied as a function of the free ATP-actin monomer concentrations, C_T. The exact analytical expressions are found to be in perfect consistency with Brownian dynamics simulations. Likewise, we find that the length diffusion coefficient is peaked near the critical concentration, C_(T, cr). It is, therefore, expected that the dependence of length diffusivity on ATP-actin monomer concentrations is utilized to analyze the surprising experiments on the length fluctuations of individual actin filaments.
机译:通过理论分析和布朗动力学模拟,研究了单肌动蛋白丝与三磷酸腺苷(ATP)水解的聚合动力学。布朗动力学模拟最近已用于研究长丝的生长行为,该行为是游离肌动蛋白单体浓度C_T的函数,该浓度与相关实验一致。在本研究中,ATP帽的长度和长度扩散率均作为游离ATP-肌动蛋白单体浓度C_T的函数进行研究。发现确切的分析表达式与布朗动力学仿真完全一致。同样,我们发现长度扩散系数在临界浓度C_(T,cr)附近达到峰值。因此,期望利用长度扩散率对ATP-肌动蛋白单体浓度的依赖性来分析关于单个肌动蛋白丝的长度波动的令人惊讶的实验。

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