Abstract
Solvent features of water in aqueous solutions of 16 free amino acids at different concentrations were characterized by the solvent comparison method. The solvent features include solvent dipolarity/polarizability, hydrogen bonding donor acidity, and hydrogen bonding acceptor basicity. The determined solvent properties describe water activity and viscosity of aqueous solutions of amino acids. These properties also describe quantitatively the solubility of different compounds in aqueous solutions of Arg and Lys. Furthermore, melting temperatures of ribonuclease A reported in the presence of Arg-HCl, Lys-HCl, and trehalose are also well described by the solvent features of water in aqueous solutions of these small organic compounds. It is suggested that analysis of the effects of free amino acids on the stability of proteins should take into account the changes in the solvent properties of water.
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