The role of solvent polarity in the free energy of transfer of amino acid side chains from water to organic solvents.
The transfer free energies of amino acid side chains from water to N-methylacetamide have been determined and compared with those obtained from other model systems. Although the process of transfer from water to N-methylacetamide represents transfer from a lower dielectric phase to a higher dielectric phase, the transfer free energies of most of the amino acid side chains are nearly the same as those obtained from the water to ethanol system. Among the apolar side chains studied, only the transfer free energies of methionine and the aromatic side chains are apparently influenced to some extent by the polarity of the organic solvent phase. The transfer free energies of the neutral polar side chains also exhibit significant dependence on solvent polarity. The van't Hoff plots for most of the apolar side chains exhibit nonlinear curves, indicating that the enthalpy of transfer from water to N-methylacetamide is temperature-dependent. It is suggested that to assess the contribution of the hydrophobic free energy to the stability of globular proteins, it is probably not necessary to account for variation in the internal environment of the protein.
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D000081:Acetamides; D000596:Amino Acids; D004735:Energy Transfer; D006860:Hydrogen Bonding; D012997:Solvents; D013696:Temperature; D013816:Thermodynamics
D000081:Acetamides; D000596:Amino Acids; D012997:Solvents; C018595:N-methylacetamide