Stochastic strategy to analyze protein folding

We propose a stochastic approach to combine methods from computational physics and Tsallis statistics in order to analyze the potential energy hypersurface of the proteins. This approach enables us to study protein folding by the topology of the energy hypersurface close to the native structures. As a bonus, this stochastic procedure allows us to obtain some of the possible intermediate states of protein folding. In particular, we describe results which suggest that the enthalpy drives the process of protein folding close to the native state. Finally, we propose an alternative view of the process of protein folding.