Thermal denaturation of collagen analyzed by isoconversional method
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Updated: Jul 11, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Sergey Vyazovkin1, Luc Vincent, Nicolas Sbirrazzuoli
1Department of Chemistry, University of Alabama at Birmingham, Birmingham, AL 35294, USA. vyazovkin@uab.edu
Abstract:
An isoconversional method is proposed to be used for evaluating activation energy of protein denaturation. Applied to DSC data on collagen denaturation, the method yields an activation energy that decreases throughout the process. The Lumry-Eyring model gives an explanation for this decrease and affords estimates for the enthalpy of the reversible step and the activation energy of the irreversible step of denaturation. The reversible unfolding is detectable by multi-frequency temperature-modulated DSC.
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