Kinetic analysis methods applied to single motor protein trajectories†,Physical Chemistry Chemical Physics

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Kinetic analysis methods applied to single motor protein trajectories†
Physical Chemistry Chemical Physics ( IF 2.9 ) Pub Date : 2018-07-02 00:00:00 , DOI: 10.1039/c8cp03056a
A. L. Nord _{1,

2,

3,

4,

5} , A. F. Pols _{6,

7,

8,

9} , M. Depken _{6,

7,

8,

9} , F. Pedaci _{1,

2,

3,

4,

5}

Affiliation

Molecular motors convert chemical or electrical energy into mechanical displacement, either linear or rotary. Under ideal circumstances, single-molecule measurements can spatially and temporally resolve individual steps of the motor, revealing important properties of the underlying mechanochemical process. Unfortunately, steps are often hard to resolve, as they are masked by thermal noise. In such cases, details of the mechanochemistry can nonetheless be recovered by analyzing the fluctuations in the recorded traces. Here, we expand upon existing statistical analysis methods, providing two new avenues to extract the motor step size, the effective number of rate-limiting chemical states per translocation step, and the compliance of the link between the motor and the probe particle. We first demonstrate the power and limitations of these methods using simulated molecular motor trajectories, and we then apply these methods to experimental data of kinesin, the bacterial flagellar motor, and F₁-ATPase.

中文翻译：

动力学分析方法应用于单个运动蛋白轨迹†

分子马达将化学或电能转换为线性或旋转的机械位移。在理想情况下，单分子测量可以在空间和时间上解析电动机的各个步骤，从而揭示了潜在的机械化学过程的重要特性。不幸的是，步骤通常很难解决，因为它们被热噪声掩盖了。在这种情况下，仍然可以通过分析记录的迹线中的波动来恢复机械化学的细节。在这里，我们扩展了现有的统计分析方法，提供了两个新途径来提取电机步长，每个易位步骤的限速化学状态的有效数量以及电机和探针颗粒之间的连接顺应性。₁ -ATP酶。

更新日期：2018-07-02

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