Abstract
Small monomeric proteins from mesophilic and thermophilic organisms were studied. They have close structural and physical and chemical properties but vary in thermal stability. A thermodynamic analysis of heat unfolding was made and integral enthalpy of unfolding (Δ H unf), heat capacity of hydration (Δ C p hyd) and enthalpy of hydration (Δ H hyd) and of the buried surface area (ΔASA) of nonpolar and polar groups as well as the enthalpy of disruption of intramolecular interaction (Δ H int in gas phase) at 298 K were determined. The absence of correlation between protein thermostability and energetic components suggests that regulatory mechanism of protein thermal stabilization has entropic nature.
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