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We consider two types of Go models of a protein (crambin) and study theirkinetics through molecular dynamics simulations. In the first model, theresidue -- residue contact interactions are selected based on a cutoffdistance, $R_c$, between the C$_\alpha$ atoms. The folding times depend on thevalue of $R_c$ strongly and non-monotonically due to the interplay betweenfrustration and the free energy barrier for folding. This indicates a need fora physically determined set of native contacts that takes into account all theresidual atoms. %%. One may accomplish it This can be accomplished byconsidering the van der Waals radii of the atoms and checking if %%the atomsoverlap. they are found within a proper range of the van der Waals attraction.In the second model, non-native attractive contacts are added to the system.This leads to bad foldability. However, for a small number of such extracontacts there is a slight acceleration in the kinetics of folding.Comment: to appear in Int. J. Mod. Phys.

THE RANGE OF THE CONTACT INTERACTIONS AND THE KINETICS OF THE GO MODELS OF PROTEINS