Palecz Bartlomiej
Department of Physical Chemistry, University of Lodz, 90-236 Lodz, Pomorska 165, Poland.
J Am Chem Soc. 2005 Dec 21;127(50):17768-71. doi: 10.1021/ja054407l.
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.
通过量热法在298.15 K的温度下测量了L-α-脯氨酸、L-α-酪氨酸、L-α-色氨酸、L-α-组氨酸、L-α-精氨酸、L-α-赖氨酸、L-天冬氨酸和L-α-谷氨酸在尿素水溶液中的溶解焓。利用溶解焓值确定了天然氨基酸两性离子与水溶液中尿素分子之间的焓非均相配对相互作用系数。根据氨基酸侧链的疏水或亲水效应来解释这些系数，这些效应影响了氨基酸与水中极性尿素分子的相互作用。
