Identification of Characteristic Protein Folding Channels in a Coarse-Grained Hydrophobic-Polar Peptide Model
Soft Condensed Matter
2009-11-13 v1
Abstract
Folding channels and free-energy landscapes of hydrophobic-polar heteropolymers are discussed on the basis of a minimalistic off-lattice coarse-grained model. We investigate how rearrangements of hydrophobic and polar monomers in a heteropolymer sequence lead to completely different folding behaviors. Studying three exemplified sequences with the same content of hydrophobic and polar residues, we can reproduce within this simple model two-state folding, folding through intermediates, as well as metastability.
Keywords
Cite
@article{arxiv.0710.4927,
title = {Identification of Characteristic Protein Folding Channels in a Coarse-Grained Hydrophobic-Polar Peptide Model},
author = {Stefan Schnabel and Michael Bachmann and Wolfhard Janke},
journal= {arXiv preprint arXiv:0710.4927},
year = {2009}
}
Comments
26 pages, 6 figures