Thermodynamics of protein denaturation at high temperatures more than 100℃

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The heat-denaturation of proteins is usually irreversible at higher temperatures than around 70℃, because of aggregation after heat denaturation. Therefore, their thermodynamic characteristics are less well understood at the temperatures more than 70℃. In this study, we found that SH-free CutA1 mutant from E. coli and its hydrophobic mutants show very good reversibility of heat denaturation at pH 9. The denaturation temperatures of the hydrophobic mutants were 90-115℃. Then, we succeeded to experimentally obtain the thermodynamic parameters of protein denaturation over 100℃ by DSC.