Transfer Energies of DL-Phenylalanine in Aqueous N,N-Dimethylformamide

The solubilities of DL-Phenylalanine change with increasing concentration of N,N-dimethylformamide (DMF) solution. The solubilities of DL-Phenylalanine were measured by "formol titration" in temperature range from 288.15 to 308.15 K. Variation of solubility helps to measure the changes of the thermodynamic parameters, as a result relative stability of amino acid molecules change in solution. Amino acid molecules remain as zwitterion in aqueous DMF solution. Three major types of interaction are main responsible for relative stability of amino acid molecules in solution. These are cavity interaction, dipole-dipole interaction and chemical interaction. These interactions are changed with increasing concentration of DMF in solution. The thermodynamics transfer energetics were measured and presented the results in graphically and explained the practical observations.