Toy model studies of soliton-mediated protein folding and conformation changes

School of Physics and Astronomy, Tel Aviv University - 69978 Tel Aviv, Israel

Received: 7 April 1998
Accepted: 10 June 1999

Abstract

We suggest that folding and conformation changes of proteins may be mediated via interaction with solitons which propagate along the molecular chain. A simple toy model is presented in which a Sine-Gordon field interact with another field ϕ corresponding to the conformation angles of the protein. We demonstrate how a soliton carries this field over energy barriers and consequently enhances the rate of the folding process. The soliton compensate for its energy loss by pumping the energy gained by the folded field. This scenario does not change significantly even in the presence of dissipation and imposed disorder. Our results of the toy model hint that a similar role might be played by solitons in real protein chains.