Nonlinear conformation of secondary protein folding

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 ${\varphi }^4$ 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.

6 pages, 1 figure

References in corpus (3)

• Nonlinearity-induced conformational instability and dynamics of biopolymers
• Anharmonic oscillation effect on the Davydov-Scott monomer in thermal bath
• The effects of bio-fluid on the internal motion of DNA