Nonlinear conformation of secondary protein folding

TL;DR

This paper introduces a nonlinear model for secondary protein folding dynamics using the Sine-Gordon equation and $^4$ interactions, highlighting how nonlinearity influences folding pathways and speed.

Contribution

It presents a novel nonlinear conformational model based on matter interactions and symmetry breaking, differing from previous linear backbone approaches.

Findings

Nonlinear backbone modeled by Sine-Gordon equation.

Nonlinear sources induce alternative folding pathways.

Nonlinearity decreases folding speed.

Abstract

A model to describe the mechanism of conformational dynamics in secondary protein based on matter interactions is proposed. The approach deploys the lagrangian method by imposing certain symmetry breaking. The protein backbone is initially assumed to be nonlinear and represented by the Sine-Gordon equation, while the nonlinear external bosonic sources is represented by $\phi^4$ interaction. It is argued that the nonlinear source induces the folding pathway in a different way than the previous work with initially linear backbone. Also, the nonlinearity of protein backbone decreases the folding speed.