Random Matrix approach to collective behavior and bulk universality in protein dynamics

Abstract

Covariance matrices of amino acid displacements, commonly used to characterize the large-scale movements of proteins, are investigated through the prism of Random Matrix Theory. Bulk universality is detected in the local spacing statistics of noise-dressed eigenmodes, which is well described by a Brody distribution with parameter $\beta \simeq 0.8$. This finding, supported by other consistent indicators, implies a novel quantitative criterion to single out the collective degrees of freedom of the protein from the majority of high-energy, localized vibrations.

4 pages, 7 figures

References in corpus (2)

• Anharmonicity and self-similarity of the free energy landscape of protein G
• Nearest-neigbor spacing distributions of the beta-Hermite ensemble of random matrices

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