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Updated: Aug 16, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
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Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen

Published on: March 4, 2017

Differential scanning microcalorimetry study of the thermal denaturation of haemoglobin

Anna Michnik1, Zofia Drzazga, Aneta Kluczewska

  • 1University of Silesia, A. Chełkowski' Institute of Physics, Department of Medical Physics, ul. Uniwersytecka 4, 40-007 Katowice, Poland. michnik@us.edu.pl

Biophysical Chemistry
|August 2, 2005
PubMed

A study of thermal denaturation of human haemoglobin A0 (HbA0) and methaemoglobin (mHb) was carried out by differential scanning calorimetry. DSC haemoglobin profiles were scan rate dependent and only partly reversible. Thermal unfolding of protein was analysed with the use of both equilibrium thermodynamic and kinetic approaches. The fittings based on the simple equilibrium/dissociation model were good and much more satisfactory than those based on "fully-kinetic" models. However the presence of some kinetic distortion during the unfolding process should be noted due to the scan-rate effect on DSC transitions. The calculated first-order kinetic constant for mHb was higher by two orders than the one for HbA0 (stabilised form). The average activation energy for HbA0 was found to be 289 +/- 28 kJ M-1 while for mHb it was about 100 kj M-1 lower.

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