Thermodynamics of Dipeptides in Water. Influence of the hydrophobic forces of the side-chains on the dissociation processes for some series of dipeptides

A calorimetric study has been carried out on the dissociation processes in water of both the free α-amino group belonging to the amino terminal residue and the free α-carboxyl groups belonging to the carboxyl terminal residue for a series having phenylalanine as the first common term. These thermodynamic quantities have been compared with those of the proton dissociation processes related to the same groups of the corresponding singleα-amino acids. The dissociation process values of this series have also been considered in connection with those obtained from others series of dipeptides previously studied, in an effort to compare the alkyl groups and benzene ring hydrophobic effects on the salvation processes of the zwitterions, undissociated molecules and ionic forms. This revised version was published online in August 2006 with corrections to the Cover Date.