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The thermodynamics of the small SH3 protein domain is studied by means of asimplified model where each bead-like amino acid interacts with the othersthrough a contact potential controlled by a 20x20 random matrix. Good foldingsequences, characterized by a low native energy, display three mainthermodynamical phases, namely a coil-like phase, an unfolded globule and afolded phase (plus other two phases, namely frozen and random coil, populatedonly at extremes temperatures). Interestingly, the unfolded globule has someregions already structured. Poorly designed sequences, on the other hand,display a wide transition from the random coil to a frozen state. Thecomparison with the analytic theory of heteropolymers is discussed

Thermodynamic features characterizing good and bad folding sequences obtained using a simplified off-lattice protein model