Statistical thermodynamical treatment of protein unfolding

Abstract

The statistical thermodynamical model of protein structure according to Ikegami (Biophys. Chem. 6, 117 (1977] has been applied to scanning calorimetric investigations of nine globular proteins. The proteins show unique properties with respect to bond energy, chain entropy and cooperative energy but individual differences with respect to the number of noncovalent bonds and a hydrophobicity parameter. The parameters specifying protein structure are correlated with experimentally determined heat capacity changes. The treatment is suited for prediction of structural parameters as shown by the alpha-lactalbumin example.