Protein Folding

The simplified model for protein folding introduced by Levitt and Warshel1 is now emerging as the method of choice for studying protein folding. Our subsequent studies in this direction focus on the development of effective ways for using the simplified model in rigorous evaluation of the free energies of the corresponding all-atom model2. More recently we started to focus on the electrostatic energetics of the simplified model, starting to generate a general electrostatically enhanced coarse grained (CG) model (3,4). The electrostatic features allowed us to obtain very reasonable results for the absolute folding energy of wide class of proteins.