Abstract
The primitive model for ionic solutions combined with the hypernetted chain approximation (HNC) is applied to study spatial correlations in aqueous solutions of ionized globular proteins. The accuracy of the theory is verified by comparison with results of a parallel Monte Carlo simulation. Good agreement of the theoretical results with the interprotein partial structure factors measured in cytochrome c solutions confirms that the model provides a satisfactory description of solute—solute interactions at various degrees of ionization and at different protein and simple electrolyte concentrations. Application of the proposed model in studies of thermodynamic behavior of protein solutions is suggested.
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