The Glass-like Structure of Globular Proteins and the Boson Peak

TL;DR

This paper explores the Boson peak in globular proteins, linking it to a mechanical instability in their energy landscape, and suggests this instability is crucial for their biological functions.

Contribution

It applies Euclidean random matrix theory to explain the Boson peak in proteins, revealing a mechanical instability underlying their vibrational spectra.

Findings

Boson peak in proteins is explained by a mechanical instability.

Energy landscape analysis links vibrational anomalies to protein function.

The approach unifies understanding of vibrational spectra in proteins and glasses.

Abstract

Vibrational spectra of proteins and topologically disordered solids display a common anomaly at low frequencies, known as Boson peak. We show that such feature in globular proteins can be deciphered in terms of an energy landscape picture, as it is for glassy systems. Exploiting the tools of Euclidean random matrix theory, we clarify the physical origin of such anomaly in terms of a mechanical instability of the system. As a natural explanation, we argue that such instability is relevant for proteins in order for their molecular functions to be optimally rooted in their structures.