We assume that the protein folding process follows two autonomous steps: the conformational search for the native, mainly ruled by the hydrophobic effect; and, the final adjustment stage, which eventually gives stability to the native. Our main tool of investigation is a 3D lattice model provided with a ten-letter alphabet, the stereochemical model. This model was conceived for Monte Carlo (MC) simulations when one keeps in mind the kinetic behavior of protein-like chains in solution. In order to characterize the folding characteristic time (τ) by two distinct sampling methods, first we present two sets of 10 3 MC simulations for a fast protein-like sequence. For these sets of folding times, τ and τ q were obtained with the application of the standard Metropolis algorithm (MA), and a modified algorithm (M q A). The results for τ q reveal two things: i) the hydrophobic chain-solvent interactions plus a set of inter-residues steric constraints are enough to emulate the first stage of the process: for each one of the 10 3 MC performed simulations, the native is always found without exception, ii) the ratio τ q /τ≅1/3 suggests that the effect of local thermal fluctuations, encompassed by the Tsallis weight, provides an innate efficiency to the chain escapes from energetic and steric traps. A physical insight is provided. Our second result was obtained through a set of 600 independent MC simulations performed with the M q A method applied to a set of 200 representative targets (native structures). The results show how structural patterns modulate τ q , which cover four orders of magnitude in the temporal scale. The third, and last result, was obtained from a special kind of simulation for those same 200 targets, we simulated their stability. We obtained a strong correlation (R=0.85) between the hydrophobic component of protein stability and the folding rate: the faster is the protein to find the native, larger is the hydrophobic component of its stability. This final result suggests that the hydrophobic interactions could not be a general stabilizing factor for proteins.