# Universality of fold-encoded localized vibrations in enzymes

## TL;DR

This study reveals that enzymes universally utilize localized, structure-encoded vibrations in the picosecond range to facilitate catalysis, providing a microscopic understanding of enzyme efficiency across diverse structures.

## Contribution

The paper introduces a mathematical framework demonstrating the universality of fold-encoded localized vibrations in enzymes, linking structure to catalytic function.

## Key findings

- Localized vibrations are optimally coupled to reaction coordinates.
- Universality demonstrated across over 900 enzyme structures.
- Provides microscopic rationale for active site compactness.

## Abstract

Enzymes speed up biochemical reactions at the core of life by as much as 15 orders of magnitude. Yet, despite considerable advances, the fine dynamical determinants at the microscopic level of their catalytic proficiency are still elusive. In this work, we use a powerful mathematical approach to show that rate-promoting vibrations in the picosecond range, specifically encoded in the 3D protein structure, are localized vibrations optimally coupled to the chemical reaction coordinates at the active site. The universality of these features is demonstrated on a pool of more than 900 enzyme structures, comprising a total of more than 10,000 experimentally annotated catalytic sites. Our theory provides a natural microscopic rationale for the known subtle structural compactness of active sites in enzymes.