Conformation changes and protein folding induced by \phi^4 interaction

TL;DR

This paper proposes a theoretical model using  interaction and symmetry breaking to describe protein conformational dynamics and folding pathways, linking nonlinear sources to internal hydrogen bonds and protein structure changes.

Contribution

It introduces a novel -based Lagrangian model for protein folding, incorporating symmetry breaking and nonlinear sources to explain conformational changes.

Findings

Model reproduces previous results on protein folding.

Folding pathways depend on nonlinear source strength.

Internal hydrogen bonds modeled as interactions with nonlinear sources.

Abstract

A model to describe the mechanism of conformational dynamics in protein based on matter interactions using lagrangian approach and imposing certain symmetry breaking is proposed. Both conformation changes of proteins and the injected non-linear sources are represented by the bosonic lagrangian with an additional \phi^4 interaction for the sources. In the model the spring tension of protein representing the internal hydrogen bonds is realized as the interactions between individual amino acids and nonlinear sources. The folding pathway is determined by the strength of nonlinear sources that propagate through the protein backbone. It is also shown that the model reproduces the results in some previous works.