Figure 10: Gibbs free energy of unfolding, or conformational stability, of homologous extremophilic proteins. The work required to disrupt the native state is plotted as a function of temperature. The high stability of the thermophilic protein is reached by lifting the curve towards higher free energy values, whereas the low stability of the psychrophilic proteins corresponds to a global collapse of the bell-shaped stability curve. Adapted from [160].