  In this study, the additional heat capacity which appear during the water
dissociation of the proteins that are one of the soft materials, have been
considered by the statistical mechanical methods. For this purpose, taking the
electric field E and total dipole moment M as the thermodynamical variables and
starting with the first law of thermodynamics an equation which reveals the
thermodynamical relation between the additional heat capacity in effective
electric field and the additional heat capacity at the constant total dipole
moment, has been obtained. It is found that, the difference between the heat
capacities depends linearly on the temperature. To bring up the hydration
effect during the folding and unfolding of the proteins the physical properties
of the apolar dissociation have been used. In the model used for this purpose;
the folding and unfolding of the proteins in the formed electric field medium
have been established on this basis. In this study with the purpose of
revealing the additional effect to the heat capacity, the partition functions
for the proteins which have been calculated in single protein molecule approach
by A. Bakk, J.S. Hoye and A. Hansen; Physica A, 304, (2002), 355-361 have been
taken in order to obtain the free energy. In this way, the additional free
energy has been related to the heat capacities. By calculating the heat
capacity in the effective electric field theoretically and taking the heat
capacity at constant total dipole moment from the experimental data, the
outcomes of the performed calculations have been investigated for Myoglobin and
other proteins.
