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We assume that the protein folding process follows two autonomous steps: theconformational search for the native, mainly ruled by the hydrophobic effect;and, the final adjustment stage, which eventually gives stability to thenative. Our main tool of investigation is a 3D lattice model provided with aten-letter alphabet, the stereochemical model. This model was conceived forMonte Carlo (MC) simulations when one keeps in mind the kinetic behavior ofprotein-like chains in solution. In order to characterize the foldingcharacteristic time ({\tau}) by two distinct sampling methods, first we presenttwo sets of 10^{3} MC simulations for a fast protein-like sequence. For thesesets of folding times, {\tau} and {\tau}_{q} were obtained with the applicationof the standard Metropolis algorithm (MA), and a modified algorithm (M_{q}A).The results for {\tau}_{q}reveal two things: i) the hydrophobic chain-solventinteractions plus a set of inter-residues steric constraints are enough toemulate the first stage of the process: for each one of the 10^{3} MC performedsimulations, the native is always found without exception, ii) the ratio{\tau}_{q}/{\tau}~1/3 suggests that the effect of local thermal fluctuations,encompassed by the Tsallis weight, provides an innate efficiency to the chainescapes from energetic and steric traps. ...

Entropic formulation for the protein folding process: hydrophobic stability correlates with folding rates