Investigation of Some of the Thermodynamical Quantities of Proteins by Statistical Mechanical Methods

TL;DR

This paper explores how enthalpy and Gibbs energy change with temperature during protein dissolution in water using statistical thermodynamics, fitting theoretical models to experimental data within 265-350 K.

Contribution

It introduces a semi-phenomenological model incorporating electric field and dipole moments to analyze protein thermodynamics, extending previous methods with a modified partition function.

Findings

Variations of enthalpy and Gibbs energy with temperature were characterized.

The model successfully fit experimental data from Privalov's studies.

Insights into protein stability and dissolution energetics were obtained.

Abstract

In this study, variations with respect to temperature of the increments of enthalpy and Gibbs energy, arising in the dissolution of proteins in water, have been investigated by the methods of statistical thermodynamics. In this formalism, effective electric field E and total dipole moment M are taken as thermodynamical variable. In obtaining the free energy the partition function given by A. Bakk, J.S. Hoye and A. Hansen; Physica A, 304, (2002), 355-361 has been used in a modified form. In the constructed semi-phenomenological theory, the experimental data are taken from the study of Privalov [1,2] and the relevant parameters have been found by fitting to the experimental curves. The variations of the increments of enthalpy and Gibbs energy have been investigated in the temperature range 265-350 K.