Life ticks as fast as how proteins move. Computationally expensive molecular dynamics simulation has been the only theoretical tool to gauge the time and sizes of these motions, though barely to their slowest ends. Here, we convert a computationally cheap elastic network model (ENM) into a molecular timer and sizer to gauge the slowest functional motions of structured biomolecules. Quasi-harmonic analysis, fluctuation profile matching, and the Wiener-Khintchine theorem are used to define the "time periods," t, for anharmonic principal components (PCs), which are validated by nuclear magnetic resonance (NMR) order parameters. The PCs with their respective "time periods" are mapped to the eigenvalues (λENM) of the corresponding ENM modes. Thus, the power laws t(ns) = 56.1λENM-1.6 and σ2(Å2) = 32.7λENM-3.0 can be established allowing the characterization of the timescales of NMR-resolved conformers, crystallographic anisotropic displacement parameters, and important ribosomal motions, as well as motional sizes of the latter.

中文翻译：

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生物大分子运动的高效计时器和尺寸测定器。

生命的proteins动与蛋白质的运动一样快。计算上昂贵的分子动力学模拟是衡量这些运动的时间和大小的唯一理论工具，尽管这些运动几乎没有达到最慢的目的。在这里，我们将计算上便宜的弹性网络模型（ENM）转换为分子计时器和定径器，以测量结构化生物分子最慢的功能运动。准谐波分析，波动轮廓匹配和Wiener-Khintchine定理用于定义非周期主成分（PC）的“时间段” t，该时间段已通过核磁共振（NMR）阶次参数进行了验证。具有各自“时间段”的PC被映射到相应ENM模式的特征值（λENM）。因此，幂律t（ns）=56.1λENM-1.6和σ2（Å2）=32.7λENM-3。