Enthalpic pair interaction coefficient between zwitterions of L-alpha-amino acids and urea molecule as a hydrophobicity parameter of amino acid side chains |
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Authors: | Palecz Bartlomiej |
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Institution: | Department of Physical Chemistry, University of Lodz, 90-236 Lodz, Pomorska 165, Poland. paleczb@uni.lodz.pl |
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Abstract: | Dissolution enthalpies of L-alpha-proline, L-alpha-tyrosine, L-alpha-tryptophan, L-alpha-histidyne, L-alpha-arginine, L-alpha-lysine, L-aspartic acid, and L-alpha-glutamic acid in aqueous solutions of urea have been measured by calorimetry at a temperature of 298.15 K. The values of dissolution enthalpy were used to determine enthalpic heterogeneous pair interaction coefficients between the zwitterions of the natural amino acids and a molecule of urea in water solution. These coefficients were interpreted in terms of the hydrophobic or hydrophilic effects of the side chains of amino acids on their interactions with a polar molecule of urea in water. |
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