  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.
