Abstract
Thermodynamic and transport properties of aqueous solutions of 13 amino acids at 298.15 K are analyzed in relation to the structure of the side chains of the biomolecules on the basis of the newly obtained and published data. The standard enthalpies of solution (ΔsolH0), partial molar volumes (V2,φ0), and partial molar contributions to the molar Gibbs free energy of activation of the viscous flow (Δμ20≠) were determined for the amino acids in water. Correlation equations were suggested to describe the relationship between the enthalpy characteristics of hydration of amino acids, viscous flow parameters, and bulk properties of their aqueous solutions.
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