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Abstract <p>The enthalpies of interaction of a solution of Tyr-Pro hydrochloride with HCl at a temperature of 298.15&#xa0;K and ionic strength values of 0.25, 0.5, and 0.75&#xa0;M (background electrolyte KCl) were measured using a calorimetric method. The stepwise dissociation constants of Tyr-Pro were determined using a potentiometric method at a temperature of 298.15&#xa0;K and a solution ionic strength of 0.2&#xa0;M (background electrolyte KCl). The following values were obtained p<i>K</i><sub>1</sub>&#xa0;= 2.87 ± 0.05, p<i>K</i><sub>2</sub>&#xa0;= 7.51 ± 0.05, and p<i>K</i><sub>3</sub>&#xa0;= 9.79 ± 0.05. The enthalpies of stepwise dissociation of the dipeptide were calculated using the universal program HEAT. Standard thermodynamic characteristics have been calculated (Δ<sub>r</sub><i>H</i>°, Δ<sub>r</sub><i>G</i>°, Δ<sub>r</sub><i>S</i>°) acid-base reactions in aqueous solutions of Tyr-Pro. The influence of the background electrolyte concentration on the peptide dissociation enthalpy is considered.</p>

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Thermodynamic Characteristics of Protolytic Equilibriums Involving Tyrosyl-Proline

  • 期刊论文

  • 发表日期：

    2025年5月27日

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  • P. D. Krutov,
  • O. N. Krutova,
  • S. A. Bychkova,
  • M. I. Bazanov,
  • V. V. Chernikov,
  • E. E. Kiptikova

摘要

Abstract

The enthalpies of interaction of a solution of Tyr-Pro hydrochloride with HCl at a temperature of 298.15 K and ionic strength values of 0.25, 0.5, and 0.75 M (background electrolyte KCl) were measured using a calorimetric method. The stepwise dissociation constants of Tyr-Pro were determined using a potentiometric method at a temperature of 298.15 K and a solution ionic strength of 0.2 M (background electrolyte KCl). The following values were obtained pK1 = 2.87 ± 0.05, pK2 = 7.51 ± 0.05, and pK3 = 9.79 ± 0.05. The enthalpies of stepwise dissociation of the dipeptide were calculated using the universal program HEAT. Standard thermodynamic characteristics have been calculated (ΔrH°, ΔrG°, ΔrS°) acid-base reactions in aqueous solutions of Tyr-Pro. The influence of the background electrolyte concentration on the peptide dissociation enthalpy is considered.