  Background: Many attempts have been made to resolve in time the folding of
model proteins in computer simulations. Different computational approaches have
emerged. Some of these approaches suffer from the insensitivity to the
geometrical properties of the proteins (lattice models), while others are
computationally heavy (traditional MD).
  Results: We use a recently-proposed approach of Zhou and Karplus to study the
folding of the protein model based on the discrete time molecular dynamics
algorithm. We show that this algorithm resolves with respect to time the
folding --- unfolding transition. In addition, we demonstrate the ability to
study the coreof the model protein.
  Conclusion: The algorithm along with the model of inter-residue interactions
can serve as a tool to study the thermodynamics and kinetics of protein models.
