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单分子力学记录分析:在肌动蛋白-肌球蛋白相互作用中的应用。

Analysis of single-molecule mechanical recordings: application to acto-myosin interactions.

作者信息

Knight A E, Veigel C, Chambers C, Molloy J E

机构信息

Biology Department, University of York, P.O. Box 373, York YO10 5YW, UK.

出版信息

Prog Biophys Mol Biol. 2001;77(1):45-72. doi: 10.1016/s0079-6107(01)00010-4.

DOI:10.1016/s0079-6107(01)00010-4
PMID:11473786
Abstract

Several laboratories have now developed methods to make single-molecule mechanical recordings from interacting pairs of biological molecules. The mechanical work done (product of force and distance) by a single biomolecular interaction is usually of the same order as thermal energy. Recordings made from non-processive, intermittently interacting, molecular motors such as acto-myosin therefore contain a large background of thermal noise. We have applied Page's test to analyse mechanical interactions between muscle myosin II's and F-actin recorded using an optical tweezers based single-molecule mechanical transducer. We compare Page's test with other variance-based methods and find it to be a robust method for analysing both simulated and real data sets. We discuss some of the problems associated with automatic detection of transient mechanical events in noisy data signals, and show that if the start and end points of individual events are known accurately then the events may be synchronised and combined to give more detailed information about different mechanical states.

摘要

现在有几个实验室已经开发出方法,可对相互作用的生物分子对进行单分子力学记录。单个生物分子相互作用所做的机械功(力与距离的乘积)通常与热能处于同一量级。因此,从非持续性、间歇性相互作用的分子马达(如肌动蛋白 - 肌球蛋白)进行的记录包含大量的热噪声背景。我们应用佩奇检验来分析使用基于光镊的单分子力学换能器记录的肌肉肌球蛋白II与F - 肌动蛋白之间的力学相互作用。我们将佩奇检验与其他基于方差的方法进行比较,发现它是一种分析模拟数据集和真实数据集的稳健方法。我们讨论了与在有噪声的数据信号中自动检测瞬态力学事件相关的一些问题,并表明如果能准确知道各个事件的起点和终点,那么这些事件就可以同步并合并,以给出关于不同力学状态的更详细信息。

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