Sequence-based study of two related proteins with different folding behaviors
Biomolecules
2007-05-23 v1 Soft Condensed Matter
Abstract
ZSPA-1 is an engineered protein that binds to its parent, the three-helix-bundle Z domain of staphylococcal protein A. Uncomplexed ZSPA-1 shows a reduced helix content and a melting behavior that is less cooperative, compared with the wild-type Z domain. Here we show that the difference in folding behavior between these two sequences can be partly understood in terms of an off-lattice model with 5-6 atoms per amino acid and a minimalistic potential, in which folding is driven by backbone hydrogen bonding and effective hydrophobic attraction.
Cite
@article{arxiv.q-bio/0312047,
title = {Sequence-based study of two related proteins with different folding behaviors},
author = {Giorgio Favrin and Anders Irbäck and Stefan Wallin},
journal= {arXiv preprint arXiv:q-bio/0312047},
year = {2007}
}
Comments
12 pages, 5 figures