Long Proteins with Unique Optimal Foldings in the H-P Model
Computational Geometry
2007-05-23 v1 Biomolecules
Abstract
It is widely accepted that (1) the natural or folded state of proteins is a global energy minimum, and (2) in most cases proteins fold to a unique state determined by their amino acid sequence. The H-P (hydrophobic-hydrophilic) model is a simple combinatorial model designed to answer qualitative questions about the protein folding process. In this paper we consider a problem suggested by Brian Hayes in 1998: what proteins in the two-dimensional H-P model have unique optimal (minimum energy) foldings? In particular, we prove that there are closed chains of monomers (amino acids) with this property for all (even) lengths; and that there are open monomer chains with this property for all lengths divisible by four.
Cite
@article{arxiv.cs/0201018,
title = {Long Proteins with Unique Optimal Foldings in the H-P Model},
author = {Oswin Aichholzer and David Bremner and Erik D. Demaine and Henk Meijer and Vera Sacristán and Michael Soss},
journal= {arXiv preprint arXiv:cs/0201018},
year = {2007}
}
Comments
22 pages, 18 figures