On foldable protein-like models; a statistical-mechanical study with Monte Carlo simulations

This is study of a class of lattice polymer models which have a singular lowest-energy conformation and undergo a phase transition from the statistically random state to the unique ground state. Such foldable lattice polymers can be considered as a crude model for protein molecules. The procedure for constructing a foldable polymer model, including selection of the monomer sequence and optimization of the force field, is described. A solvation term for individual monomers was added to the pairwise contact-based potential commonly used for the lattice polymer model. It is shown that the solvation interactions of individual residues make an important contribution to the folding of protein-like models. The statistical-mechanical characteristics of the models were analyzed with the help of Monte Carlo simulations. The model provides many insights to the protein-folding problem.