  We present results of Monte Carlo computer simulations of a coarse-grained
hydrophobic-polar Go-like heteropolymer model and discuss thermodynamic
properties and kinetics of an exemplified heteropolymer, exhibiting two-state
folding behavior. It turns out that general, characteristic folding features of
realistic proteins with a single free-energy barrier can also be observed in
this simplified model, where the folding transition is primarily driven by the
hydrophobic force.
