Eur. Phys. J. E (2008) 27: 197-204
https://doi.org/10.1140/epje/i2007-10371-4

Regular Article

Dynamics of alpha helix formation in the CSAW model

¹ Zhou Pei-Yuan Center for Applied Mathematics, Tsinghua University, 100084, Beijing, China
² Physics Department, Massachusetts Institute of Technology, 02139, Cambridge, MA, USA

^* e-mail: jzlei@tsinghua.edu.cn
^** e-mail: kerson@mit.edu

Received: 10 October 2007
Accepted: 3 September 2008
Published online: 30 September 2008

Abstract

We study the folding dynamics of polyalanine ( Ala₂₀, a protein fragment with 20 residues whose native state is a single alpha helix. We use the CSAW model (conditioned self-avoiding walk), which treats the protein molecule as a chain in Brownian motion, with interactions that include hydrophobic force and internal hydrogen bonding. We find that large-scale structures form before small-scale structures, and obtain the relevant relaxation times. We find that helix nucleation occurs at two separate points on the protein chain, one near each end. The evolution of small- and large-scale structures involves different mechanisms. While the former can be described by rate equations that govern the growth of helical content, the latter is akin to the relaxation of an elastic solid.