  In this paper we investigate the role of native geometry on the kinetics of
protein folding based on simple lattice models and Monte Carlo simulations.
Results obtained within the scope of the Miyazawa-Jernigan indicate the
existence of two dynamical folding regimes depending on the protein chain
length. For chains larger than 80 amino acids the folding performance is
sensitive to the native state's conformation. Smaller chains, with less than 80
amino acids, fold via two-state kinetics and exhibit a significant correlation
between the contact order parameter and the logarithmic folding times. In
particular, chains with N=48 amino acids were found to belong to two broad
classes of folding, characterized by different cooperativity, depending on the
contact order parameter. Preliminary results based on the G\={o} model show
that the effect of long range contact interaction strength in the folding
kinetics is largely dependent on the native state's geometry.
