Long Proteins with Unique Optimal Foldings in the H-P Model
<|reference_start|>Long Proteins with Unique Optimal Foldings in the H-P Model: 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.<|reference_end|>
@article{aichholzer2002long,
    title={Long Proteins with Unique Optimal Foldings in the H-P Model},
    author={Oswin Aichholzer, David Bremner, Erik D. Demaine, Henk Meijer, Vera
  Sacrist'an, Michael Soss},
    journal={arXiv preprint arXiv:cs/0201018},
    year={2002},
    archivePrefix={arXiv},
    eprint={cs/0201018},
    primaryClass={cs.CG q-bio.BM}
}