A new method has been developed for determining the stability parameters of proteins from their heatinduced transition curves followed by observation of changes in the far-UV circular dichroism (CD). This method of analysis of the thermal denaturation curve of a protein gave values of stability parameters that not only are identical to those measured by the differential scanning calorimetry (DSC), but also are measured with the same error as that observed with a calorimeter. This conclusion has been reached from our studies of the reversible heat-induced denaturation of lysozyme and ribonuclease A at various pH values. For each protein, the conventional method of analysis of the conformational transition curve, which assumes a linear temperature dependence of the preand posttransition baselines, gave the estimate of ⌬H m - van (enthalpy change on denaturation at T m , the midpoint of denaturation) which is significantly lower than ⌬H m cal , the value obtained from DSC measurements. However, if the analysis of the same denaturation curve assumes that a parabolic function describes the temperature dependence of the pre-and posttransition baselines, there exists an excellent agreement between ⌬H m van and ⌬H m cal of the protein. The latter analysis is supported by the far-UV CD measurements of the oxidized ribonuclease A as a function of temperature, for the temperature dependence of this optical property of the protein is indeed nonlinear. Furthermore, it has been observed that, for each protein, the constant-pressure heat capacity change (⌬C p ) determined from the plots of ⌬H m van versus T m is independent of the method of analysis of the transition curve.