Abstract
The constants and enthalpies of acid dissociation of glycyl-glycyl-glycine peptide in aqueous solutions at 298.15 K and ionic strength values of 0.1, 0.5, and 1.0 M containing NaCl as a background electrolyte, were determined by potentiometry and calorimetry. The standard values of pK 1 ° and pK 2 ° constants, the change of Gibbs energy, enthalpy, and entropy for the dissociation processes were calculated. It was found that the acidic properties of the carboxylic group in aqueous solution subside upon the transition from α-amino acids to peptides due to the lower entropy effect of dissociation. It was concluded that the increase of dissociation constant of a protonated peptide amino group upon an increase in the length of its molecule is determined by entropy factor associated with the attenuation of amino group solvation.
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