Before revision:  Slightly hydrophobic cages seem to make the native structure more stable . However, not any confining potential helps folding . If the inner walls of the cage are strongly hydrophobic, a denaturation process is induced, in which the proteins partially unfold and stick to the walls .
After revision:  Slightly hydrophobic cages seem to make the native structure more stable than in the case of pure repulsive potentials, and the folding process occurs through intermediate configurations. In order to test the metastable states we analyze the free energy landscapes as a function of the configurational energy and of the end-to-end distance as an order parameter .