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.Comment: 22 pages, 18 figure