The statistical properties of protein folding in the ϕ^4 theory
arXiv:1112.4712 · doi:10.1166/jctn.2013.3175
Abstract
The statistical properties of protein folding within the ϕ^4 model are investigated. The calculation is performed using statistical mechanics and path integral method. In particular, the evolution of heat capacity in term of temperature is given for various levels of the nonlinearity of source and the strength of interaction between protein backbone and nonlinear source. It is found that the nonlinear source contributes constructively to the specific heat especially at higher temperature when it is weakly interacting with the protein backbone. This indicates increasing energy absorption as the intensity of nonlinear sources are getting greater. The simulation of protein folding dynamics within the model is also refined.
17 pages, 3 figures
References in corpus (5)
- Nonlinearity-induced conformational instability and dynamics of biopolymers
- Path Integral Methods and Applications
- Anharmonic oscillation effect on the Davydov-Scott monomer in thermal bath
- The thermodynamic properties of Davydov-Scott's protein model in thermal bath
- Conformation changes and protein folding induced by ϕ^4 interaction