Folding simulations of a three-dimensional protein model with a nonspecific hydrophobic energy function.

We show that a nonspecific hydrophobic energy function can produce protein-like folding behavior of a three-dimensional protein model of 40 monomers in the cubic lattice when the native conformation is chosen judiciously. We confirm that monomer inside/outside segregation is a powerful criterion for the selection of appropriate structures, an idea that was recently proposed with basis on a general theoretical analysis and simulations of much simpler two-dimensional models.