Evaluation of thermodynamic properties of irreversible protein thermal unfolding measured by DSC

We assessed the applicability of the extrapolation procedure at infinite scanning rate to differential scanning calorimetry (DSC) data related to irreversible protein unfolding. To this aim, an array of DSC curves have been simulated on the basis of the Lumry - Eyring model N <-> U --> F. The results obtained confirmed that when the apparent equilibrium constant K-app(T= T1/2) is lower than 3, the application of the extrapolation procedure provides accurate thermodynamic parameters. Although this procedure applies only to monomeric proteins for which the Lumry - Eyring model is a reasonable approximation, it will hopefully contribute to increase the potential of DSC in obtaining reliable thermodynamic information regarding the folding/unfolding equilibrium.