| Abstract
| - Dissolution enthalpies of l-α-proline, l-α-tyrosine, l-α-tryptophan, l-α-histidyne, l-α-arginine, l-α-lysine, l-aspartic acid, and l-α-glutamic acid in aqueous solutions of urea have been measured by calorimetryat a temperature of 298.15 K. The values of dissolution enthalpy were used to determine enthalpicheterogeneous pair interaction coefficients between the zwitterions of the natural amino acids and a moleculeof urea in water solution. These coefficients were interpreted in terms of the hydrophobic or hydrophiliceffects of the side chains of amino acids on their interactions with a polar molecule of urea in water.
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