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

O. Aichholzer, D. Bremner, E. Demaine, D. Meijer, V. Sacristán, and M. Soss

Abstract:

We explore a problem suggested by Brian Hayes in 1998: what proteins in the two-dimensional hydrophilic-hydrophobic (H-P) model have unique optimal 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 fo all lengths divisible by four. Along the way, we prove and conjecture several results about bonds in the H-P model.

Reference: O. Aichholzer, D. Bremner, E. Demaine, D. Meijer, V. Sacristán, and M. Soss. Long proteins with unique optimal foldings in the h-p model. In Proc. $17^{th}$ European Workshop on Computational Geometry CG '2001, pages 59-62, Berlin, Germany, 2001.