Backbone and Sidechain Ordering in a small Protein
Abstract
We investigate the relation between backbone and side-chain ordering in a small protein. For this purpos e we have performed multicanonical simulations of the villin headpiece subdomain HP-36, an often used to y model in protein studies. Concepts of circular statistics are introduced to analyze side-chain fluctuations. In contrast to earlier studies on homopolypeptides (Wei et al., J. Phys. Chem. B, 111 (2007) 4244) we do not find collective effects leading to a separate transition. Rather, side-chain ordering is spread over a wide temperature range. Our results indicate a thermal hierarchy of ordering events, with side-chain ordering appearing at temperatures below the helix-coil transition but above the folding transition. We conjecture that this thermal hierarchy reflects an underlying temporal order, and that side-chain ordering facilitates the search for the correct backbone topology.
Keywords
Cite
@article{arxiv.0711.4090,
title = {Backbone and Sidechain Ordering in a small Protein},
author = {Y. Wei and W. Nadler and U. H. E. Hansmann},
journal= {arXiv preprint arXiv:0711.4090},
year = {2009}
}
Comments
accepted in J. Chem. Phys