Protein folding discretized, lattice models

The simplest model for a quahtative description of protein folding is the lattice hydrophobic jolar (HP) model [12]. In this model, the continuous conformational space is reduced to discrete regular lattices and conformations of proteins are modeled as selfavoiding walks restricted to the lattice. Assuming that the hydrophobic interaction is the most essential force toward the native fold, sequences of HP proteins consist of only two types of monomers (or classes of amino acids) Amino acids with high hydrophobicity are treated as hydrophobic monomers (//), while the class of polar (or hydrophihc) residues is... 

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