Long Proteins with Unique Optimal Foldings in the H-P Model

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dc.creatorAichholzer, Oswin
dc.creatorBremner, David
dc.creatorDemaine, Erik D.
dc.creatorMeijer, Henk
dc.creatorSacristán, Vera
dc.creatorSoss, Michael
dc.date2002-01-21
dc.date.accessioned2026-07-07T03:18:04Z
dc.date.available2026-07-07T03:18:04Z
dc.descriptionIt 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.description22 pages, 18 figures
dc.identifierhttps://arxiv.org/abs/cs/0201018
dc.identifierhttp://arxiv.org/abs/cs/0201018
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/30967
dc.subjectComputational Geometry
dc.subjectBiomolecules
dc.subjectG.2; I.3.5
dc.titleLong Proteins with Unique Optimal Foldings in the H-P Model
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