Different Kinds of Protein Folding Identified with a Coarse-Grained Heteropolymer Model
Soft Condensed Matter
2009-02-17 v1 Other Condensed Matter
Abstract
Applying multicanonical simulations we investigated folding properties of off-lattice heteropolymers employing a mesoscopic hydrophobic-polar model. We study for various sequences folding channels in the free-energy landscape by comparing the equilibrium conformations with the folded state in terms of an angular overlap parameter. Although all investigated heteropolymer sequences contain the same content of hydrophobic and polar monomers, our analysis of the folding channels reveals a variety of characteristic folding behaviors known from realistic peptides.
Keywords
Cite
@article{arxiv.0902.2652,
title = {Different Kinds of Protein Folding Identified with a Coarse-Grained Heteropolymer Model},
author = {Stefan Schnabel and Michael Bachmann and Wolfhard Janke},
journal= {arXiv preprint arXiv:0902.2652},
year = {2009}
}
Comments
3 pages, 2 figures