The thermal unfolding of human carbonic anhydrase II (HCAII) has been studied by circular dichroism, UV-vis spectrophotometry, and differential scanning calorimetry (DSC). Coincidence of aggregation and tertiary structure disruption as well as fitting of DSC data showed that a two-state model can properly explain thermal unfolding of HCAII. According to this model, the average values of T* (the temperature at which k = 1/60 s -1 ), ΔH (enthalpy), and ΔE a (activation energy) are equal to 335.8 K, 698.6 kJ 3 mol -1 , and 529.0 kJ 3 mol -1 , respectively.
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