The HP model of protein folding: A challenging testing ground for Wang–Landau sampling

The hydrophobic-polar (HP) lattice protein model has gained much attention as a standard in assessing the efficiency of computational methods for protein structure prediction as well as for exploring the statistical physics of protein folding. In this work we show that Wang–Landau sampling, in connection with a suitable move set (pull moves), provides a powerful route for both the search of global energy minimum conformations and the precise determination of the density of states for HP sequences with up to 100 monomers in two and three dimensions. The main advantage of our approach lies in its general applicability to a broad range of lattice protein models that go beyond the scope of the HP model.