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Abstract
We performed thermodynamic analysis of temperature-induced unfolding of mesophilic and thermophilic proteins. It was shown that the variability in protein thermostability associated with pH-dependent unfolding or linked to the substitution of amino acid residues on the protein surface is evidence of the governing role of the entropy factor. Numerical values of conformational components in enthalpy, entropy and free energy which characterize protein unfolding in the “gas phase” were obtained. Based on the calculated absolute values of entropy and free energy, a model of protein unfolding is proposed in which the driving force is the conformational entropy of native protein, as an energy of the heat motion (T·SNC) increasing with temperature and acting as an factor devaluating the energy of intramolecular weak bonds in the transition state.
Notes
This article was originally published with errors. This version has been corrected. Please see Erratum (http://dx.doi.org/10.1080/07391102.2013.842357).