A statistical mechanical deconvolution of the differential scanning calorimetric profiles of the thermal denaturation of cyanomethemoglobin.

A differential scanning calorimetric study of the thermal unfolding of horse cyanomethemoglobin (as an irreversible protein system) was carried out in phosphate-EDTA buffer (20 mM phosphate, 1 mM EDTA) pH 7.2. The calorimetric rescanning of the protein solution was found to be irreversible and the process unfolded state --> final state appears to follow first order kinetic.