Long Proteins with Unique Optimal Foldings in the H-P Model
| dc.creator | Aichholzer, Oswin | |
| dc.creator | Bremner, David | |
| dc.creator | Demaine, Erik D. | |
| dc.creator | Meijer, Henk | |
| dc.creator | Sacristán, Vera | |
| dc.creator | Soss, Michael | |
| dc.date | 2002-01-21 | |
| dc.date.accessioned | 2026-06-02T21:40:22Z | |
| dc.description | 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. | |
| dc.description | 22 pages, 18 figures | |
| dc.identifier | https://arxiv.org/abs/cs/0201018 | |
| dc.identifier | http://arxiv.org/abs/cs/0201018 | |
| dc.identifier.uri | https://demo.dspace.org/handle/10673/1619 | |
| dc.subject | Computational Geometry | |
| dc.subject | Biomolecules | |
| dc.subject | G.2; I.3.5 | |
| dc.title | Long Proteins with Unique Optimal Foldings in the H-P Model | |
| dc.type | text |