Unfolding designable structures
Soft Condensed Matter
2009-11-11 v2 Statistical Mechanics
Abstract
Among an infinite number of possible folds, nature has chosen only about 1000 distinct folds to form protein structures. Theoretical studies suggest that selected folds are intrinsically more designable than others; these selected folds are unusually stable, a property called the designability principle. In this paper we use the 2D hydrophobic-polar lattice model to classify structures according to their designability, and Langevin dynamics to account for their time evolution. We demonstrate that, among all possible folds, the more designable ones are easier to unfold due to their large number of surface-core bonds.
Cite
@article{arxiv.cond-mat/0510393,
title = {Unfolding designable structures},
author = {Cristiano L. Dias and Martin Grant},
journal= {arXiv preprint arXiv:cond-mat/0510393},
year = {2009}
}
Comments
10 pages, 4 figures, Proceeding of the 3rd International Conference NEXT-SigmaPhi