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The thermodynamic properties of the cardiac and skeletal a-actin isoforms were studied to characterize the molecular bases of the functional differences between them with the method of differential scanning calorimetry (DSC). The thermal properties of the actin filaments were described in the presence of calcium and magnesium ions as well. Based on the calculated free energy changes the α-cardiac actin filaments appeared to be more stable in its physiologically more relevant, magnesium saturated form. The magnesium saturated form of the α-cardiac actin filaments seemed to be more stable compared to the calcium saturated form of it. The enthalpy and entropy changes could differentiate between the α-cardiac and α-skeletal actin isoforms and between the calcium and magnesium saturated cardiac actin isoforms as well. Our results can demonstrate that the few differences between the amino acid sequences of the α-actin isoforms have an influence on the thermal properties and maybe on the function of these proteins as well.

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Journal of Thermal Analysis and Calorimetry
Authors: J. Orbán, Kinga Pozsonyi, Krisztina Szarka, Szilvia Barkó, Emőke Bódis, and D. Lőrinczy


The thermodynamic properties of the ADP- and ATP-actin filaments were compared by the method of differential scanning calorimetry. The lower melting point for the ADP-F-actin filament (58.4 vs. 64.5°C for ATP-F-actin) indicated that compared to the ATP-actin filaments its structure was less resistant to heat denaturation. The detailed thermodynamic characterisation of the proteins was carried out by the analysis of the calorimetric enthalpy, the entropy and the free enthalpy changes. All of the determined parameters gave lower values to the ADP-actin filaments than to the ATP-actin filaments. The calculated values of the activation energy also demonstrated that compared to the ADP-F-actin the ATP-F-actin was thermodynamically more resistant to the denaturing effect of heat. Based on all of this information we have concluded that the actin filament prepared from ADP containing magnesium saturated actin monomers at pH 8.0 is thermodynamically less stable than the ones obtained from ATP-actin monomers.

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