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This article focuses on thermal unfolding profiles. An electron-transfer protein, soluble monoheme cytochrome c (cyt c) is among the essential redox proteins sustaining biological activity. Another fundamental way to elucidate the redox function of cyt c is to characterize its thermo-dynamic property of both oxidized and reduced forms because the redox potential is derived from the difference between these two redox states. Conventionally, there are two protein thermal-unfolding experiments. First, differential scanning calorimetric (DSC) measurements can be carried out at more than 100 degree celcius.

Studies relationship between Redox function and protein stability of cytochromes c. Denaturation temperatures and thermodynamic parameters of Redox reaction for cytochromes c; Electrochemiocal measurement to determine the relationship betwen Redox function and protein stability of cytochromes c; Experimental observation of the analysis.