Protein vibrations and their localization behaviour. A numerical scaling analysis
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Updated: Nov 8, 2025

An Analog Macroscopic Technique for Studying Molecular Hydrodynamic Processes in Dense Gases and Liquids
Published on: December 4, 2017
Felix Guischard1, Jetmir Haxhija1, Jan Kaiser1
1Institut für Physikalische Chemie, Universität Freiburg, Albertstraße 21, 79104 Freiburg im Breisgau, Germany.
Abstract:
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-1. Biophysical and biochemical implications are discussed, and the vibrational localization properties are compared to those of amorphous solids.
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