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Updated: Feb 7, 2026

Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Study of Human Fibrinogen Oxidative Modification using Differential Scanning Calorimetry
M G Gorobets1, L A Wasserman2, A V Bychkova2
1Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334, Russia. maria.g.gorobets@gmail.com.
Abstract:
For the first time, with the aid of differential scanning calorimetry, the thermal denaturation of fibrinogen under induced oxidation was studied. All fibrinogen structural elements detected by DSC (D region, αC-domain, and E region) are subjected to oxidation. Structural changes in fibrinogen molecule were characterized by the denaturation temperature, denaturation enthalpy, and van't Hoff enthalpy.
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