聚合肌动蛋白中协同磷酸盐释放测量方法的定量分析。
Quantitative analysis of approaches to measure cooperative phosphate release in polymerized actin.
机构信息
Department of Physics, Washington University, St. Louis, MO, USA.
出版信息
Biophys J. 2012 Dec 5;103(11):2369-78. doi: 10.1016/j.bpj.2012.10.032.
Abstract
We use stochastic simulations that treat several experimental probes of actin dynamics to explore the extent to which phosphate dissociation in filamentous actin may be cooperative. Phosphate time-courses from polymerization and copolymerization experiments of ATP- and ADP-actin are studied, including the effects of variations in filament-number concentration as well as single-filament depolymerization time-courses. We find that highly cooperative models are consistent with the treated experimental data. We also find that some types of experiments that are believed to provide strong constraints on the cooperativity of actin hydrolysis models do not provide such constraints.
摘要
我们使用随机模拟的方法，通过处理几种肌动蛋白动力学的实验探针来探索丝状肌动蛋白中磷酸基团解离是否具有协同性。我们研究了 ATP-和 ADP-肌动蛋白聚合和共聚实验中的磷酸时间曲线，包括纤维丝数量浓度变化以及单纤维丝解聚时间曲线的影响。我们发现高度协同模型与处理后的实验数据一致。我们还发现，一些被认为可以为肌动蛋白水解模型的协同性提供强约束的实验类型实际上并没有提供这样的约束。
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