# Gauge symmetries and structure of proteins

## TL;DR

This paper applies gauge field theory to model protein structures, introducing a novel approach that captures the protein backbone's 3D structure and dynamics through topological solitons and symmetry breaking.

## Contribution

It presents a new gauge theory-based model for protein structures, linking gauge symmetry breaking to protein folding and dynamics prediction.

## Key findings

- Reproduces protein backbone structure with 1A accuracy
- Models protein folding via gauge symmetry breaking
- Predicts protein dynamics using topological solitons

## Abstract

We discuss the gauge field theory approach to protein structure study, which allows a natural way to introduce collective degrees of freedom and nonlinear topological structures. Local symmetry of proteins and its breaking in the medium is considered, what allows to derive Abelian Higgs model of protein backbone, correct folding of which is defined by gauge symmetry breaking due hydrophobic forces. Within this model structure of protein backbone is defined by superposition of one-dimensional topological solitons (kinks), what allows to reproduce the three-dimensional structure of the protein backbone with precision up to 1A and to predict its dynamics.