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The HP model represents protein sequences by coarse-graining amino acid types as either hydrophobic (H) or polar (P). This model has been studied extensively, where the simple cubic (sc) lattice is a commonly used for simplicity and efficiency, despite a limited ability to geometrically represent protein structures. One straightforward improvement is to instead use the face-centered cubic (fcc) lattice, which offers a more realistic geometry while retaining simplicity. Using the replica-exchange Wang-Landau algorithm, the ground state energies and full density of states are predicted for a set of biologically-motivated HP sequences on the fcc lattice. A direct thermodynamic comparison is made between the folding on fcc and sc lattices, and structural properties are calculated to further examine the folding on the fcc lattice.

Comparison of Benchmark HP Model Proteins on Face-Centered Cubic and Simple Cubic Lattices using Replica-Exchange Wang-Landau Sampling