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Citation: HU Xin-Gen, YU Li, LIN Rui-Sen, FANG Ying-Ying, LI Wen-Bing. Study on Hydrophobic Self-association of Aliphatic α-amino Acids by Flow Microcalorimetry[J]. Acta Physico-Chimica Sinica, ;2006, 22(08): 1034-1039. doi: 10.3866/PKU.WHXB20060825 shu

Study on Hydrophobic Self-association of Aliphatic α-amino Acids by Flow Microcalorimetry

1.
School of Chemistry and Materials Science, Wenzhou University Zhejiang Wenzhou 325027, P. R. China;Key Laboratory for Colloid and Interface Chemistry of State Education Ministry, Shandong University, Jinan 250100, P. R. China;Department of Chemistry, Zhejiang University, Hangzhou 310027, P. R. China；

Received Date: 21 February 2006
Available Online: 7 July 2006

A chemical interaction model has been established for the hydrophobic self- association of aliphatic α- amino acids in aqueous solutions. In order to obtain the parameters of the model equation, dilution enthalpies of 5 aliphatic α- amino acids aqueous solutions have been measured at 298.15 K by flow microcalorimetry. The equilibrium constants (K), enthalpy change (ΔHm) and entropy change (ΔSm) have been determined for the equal- step association. It was found that between enthalpy and entropy exists a od compensation relationship. In addition, partial molar excess entropies of water in solutions (SE1) were calculated, and were discussed according to the hydration model for aliphatic α- amino acids. Noteworthily, the parameters in the model equation can be used to explain the homogeneous enthalpic interaction coefficients in McMillan- Mayer model to some extent.
- α-amino acids;Hydrophobic self-association;Chemical model;Dilution enthalpy;Flow microcalorimetry
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