One remarkable aspect of small globular proteins folding process is the fastness. However, different proteins of
similar sizes may paradoxically present folding rates that differ by several orders of magnitude. In the present work we
show how reliably a specific minimalist lattice model can reproduce such large range of folding characteristic times
during the search stage of the protein folding process. We select nine representative protein-like (compact) structures,
which illustrate distinct combinations of cooperative and non-cooperative structural patterns. The respective sequences of
residues are designed by a general rule, and then submitted to extensive Monte Carlo simulations to determine the
characteristic folding time of each target structure. Our results reproduce the experimentally observed exponential-like
folding kinetics --of small, two-state globular proteins, and strongly support the idea that the search mechanism for the
native structure is fully governed by the hydrophobic effect and steric constraints. The present results are achieved
through the application of nonextensive statistical mechanics.
Keywords: Protein folding, Stereochemical model, Monte Carlo, Nonextensive, Superstatistics, hydrophobic, minimalist lattice, thermodynamic, natural residues.
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