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 que...
| Principais autores: | , , , , , |
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| Outros Autores: | |
| Formato: | Artigo |
| Idioma: | en_US |
| Publicado em: |
Elsevier
2014
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| Acesso em linha: | http://hdl.handle.net/1721.1/86069 https://orcid.org/0000-0003-3803-5703 |
| Resumo: | 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. |
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