Ishii Yoshiharu, Taniguchi Yuichi, Iwaki Mitsuhiro, Yanagida Toshio
Formation of Soft Nano-Machines, CREST, JST, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.
Biosystems. 2008 Jul-Aug;93(1-2):34-8. doi: 10.1016/j.biosystems.2008.04.015. Epub 2008 May 9.
Recently developed single molecule measurements have demonstrated that the mechanisms for numerous protein functions involve thermal fluctuation, or Brownian motion. Protein interactions bias the random thermal noise in a manner such that the protein can perform its given functions. This phenomenon has been observed in molecular motor unidirectional movement where Brownian motion is used to preferentially bind the motor heads in one direction causing directional motility. This is analogous to that used by proteins in which spontaneous structural fluctuations are used to switch function. Seeing that two very different systems implement similar mechanisms suggests there exists a general scheme applied by diverse proteins that exploits thermal fluctuations in order to achieve their respective functions.
最近发展起来的单分子测量技术表明，许多蛋白质功能的机制涉及热涨落，即布朗运动。蛋白质相互作用以一种使蛋白质能够执行其特定功能的方式使随机热噪声产生偏差。这种现象在分子马达单向运动中已被观察到，其中布朗运动被用于优先在一个方向上结合马达头部，从而导致定向运动。这类似于蛋白质所采用的方式，其中自发的结构涨落被用于切换功能。鉴于两个截然不同的系统采用了相似的机制，这表明存在一种由多种蛋白质应用的通用方案，该方案利用热涨落来实现它们各自的功能。
