Institut für Physikalische Chemie, Universität Freiburg, Albertstraße 21, 79104 Freiburg im Breisgau, Germany.
Institut für Physikalische Chemie, Universität Freiburg, Albertstraße 21, 79104 Freiburg im Breisgau, Germany.
Biophys Chem. 2021 Jul;274:106594. doi: 10.1016/j.bpc.2021.106594. Epub 2021 Apr 19.
Using a classical force field, we investigate the localization properties of protein normal modes. For a set of eighteen proteins that cover five classes of increasing size, we compute the participation ratio as a measure of the spatial extent of protein vibrations. In this scaling analysis, we find extended low-frequency far-infrared and Terahertz modes, in contrast to localized high-frequency near-infrared vibrations. These regimes are separated by a broad crossover around a wave number of 260 cm. Biophysical and biochemical implications are discussed, and the vibrational localization properties are compared to those of amorphous solids.
利用经典力场，我们研究了蛋白质正常模式的局域化特性。对于涵盖五个尺寸递增类别的十八种蛋白质，我们计算了参与比作为蛋白质振动空间范围的度量。在这种标度分析中，我们发现了扩展的低频远红外和太赫兹模式，而不是局域的高频近红外振动。这些区域通过大约 260cm-1 的波数的宽交叉区分开。讨论了生物物理和生物化学的意义，并将振动局域化特性与无定形固体进行了比较。
