It is shown the non-occurrence of a correlation between the values of the denaturation temperature and those of the denaturation heat capacity change for a set of 13 proteins possessing the ‘SH3-type’ fold from both mesophilic and thermophilic microorganisms. This seems to be a rather general result, because, fixed the size and the folding pattern, the denaturation heat capacity change is a nearly constant quantity, within the uncertainty limits of experimental determinations, regardless of the thermal stability of the protein. A precise definition of the thermodynamics of the hydrophobic effect is presented to clarify that the above finding does not imply that the hydrophobic effect does not play a role in the extra-thermal stability of thermophilic and hyperthermophilic proteins.