The unraveling and control of protein stability at different temperatures is a fundamental problem in biophysics that is substantially far from being quantitatively and accurately solved, as it requires a precise knowledge of the temperature dependence of amino acid interactions. In this paper we attempt to gain insight into the thermal stability of proteins by designing a tool to predict the full stability curve as a function of the temperature for a set of 45 proteins belonging to 11 homologous families, given their sequence and structure, as well as the melting temperature (Tm) and the change in heat capacity (xcex94CP) of proteins belonging to the same family. Stability curves constitute a fundamental instrument to analyze in detail the thermal stability and its relation to the thermodynamic stability, and to estimate the enthalpic and entropic contributions to the folding free energy. In summary, our approach for predicting the protein stability curves relies on temperature-dependent statistical potentials derived from three datasets of protein structures with targeted thermal stability properties. Using these potentials, the folding free energies (xcex94G) at three different temperatures were computed for each protein. The Gibbs-Helmholtz equation was then used to predict the proteins stability curve as the curve that best fits these three points. The results are quite encouraging: the standard deviations between the experimental and predicted Tms, xcex94CPs and folding free energies at room temperature (xcex94G25) are equal to 13xc2xb0 C, 1.3 kcal/(molxc2xb0 C) and 4.1 kcal/mol, respectively, in cross-validation. The main sources of error and some further improvements and perspectives are briefly discussed.