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

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

2002-01-21

arxiv.org/abs/cs/0201018v1

Computer Science

Computational Geometry

22 pages, 18 figures

Scientific paper

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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