Thermochemical
investigation of acid-base interactions in peptide solutions |
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| Authors: | G G Gorboletova L A Kochergina |
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| Institution: | (1) Ivanovo State University of Chemistry and Technology, Ivanovo, Russia, 153000, Engels Avenue 7 |
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| Abstract: | Heat effects
of interaction of D,L-α-alanyl-D,L-α-alanine,
glycil-γ-aminobutyric acid, glycil-L-asparagine
and D,L-α-alanyl-D,L-asparagine
with KOH, LiOH and HNO3 solutions were measured by
the direct calorimetry method at 288.15, 298.15, 308.15, 318.15 K and at several
values of the ionic strength created by adding KNO3
and LiNO3.
The standard dissociation enthalpies
of the investigated ligands were obtained by the extrapolation to zero ionic
strength. The standard thermodynamic characteristics (ΔG
0
, ΔH
0 ,
ΔS
0 , ΔC
p
0)
of the processes of acid-base interaction in dipeptide solutions were calculated.
Several peculiarities of acid-base interaction reactions in the solutions
of biologically important ligands were found. The correlations between the
thermodynamic characteristics of the protolytic equilibria in the dipeptide
and aminoacids solutions and the structure of these compounds were determined. |
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| Keywords: | aminoacid calorimetry dipeptide dissociation temperature thermodynamic characteristics |
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