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<p>The conformational stability of pea vicilin was studied by high-sensitivity differential scanning calorimetry and sedimentation velocity at different pHs. It was found that vicilin completely conserved its trimeric 7S structure over the pH range from 3 to 10, and only partly dissociated into 4S subunits at pH 2 and 11. The temperature dependences of the partial heat capacity of vicilin were measured at different pHs. The pre-denaturation linear segments of these dependences were in quantitative agreement with a universal Freire function thus suggesting a native folding of the vicilin preparation. The denaturation curves of vicilin were deconvoluted into two independent cooperative transitions. This result implied the presence of two energetically different structural domains in vicilin subunits. The standard Gibbs free energies of denaturation for each domain were determined as functions of pH. These dependences were well approximated by the Harold Scheraga model, which considered the contributions of hydrogen bonds between definite ionogenic groups of a protein to its stability. The number and types of such bonds were determined. These data were generally confirmed by the analysis of the three-dimensional structure of the vicilin molecule.</p>

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Conformational stability of pea vicilin: a high-sensitivity differential scanning calorimetry study

  • 期刊论文

  • 发表日期：

    2026年4月29日

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  • Tatiana V. Burova,
  • Natalia V. Grinberg,
  • Alexander P. Moskalets,
  • Vladimir B. Tsvetkov,
  • Alevtina I. Kulebyakina,
  • Timofei E. Grigoriev,
  • Alexander S. Dubovik,
  • Irina G. Plashchina,
  • Sergey V. Bobkov,
  • Valerij Y. Grinberg

摘要

The conformational stability of pea vicilin was studied by high-sensitivity differential scanning calorimetry and sedimentation velocity at different pHs. It was found that vicilin completely conserved its trimeric 7S structure over the pH range from 3 to 10, and only partly dissociated into 4S subunits at pH 2 and 11. The temperature dependences of the partial heat capacity of vicilin were measured at different pHs. The pre-denaturation linear segments of these dependences were in quantitative agreement with a universal Freire function thus suggesting a native folding of the vicilin preparation. The denaturation curves of vicilin were deconvoluted into two independent cooperative transitions. This result implied the presence of two energetically different structural domains in vicilin subunits. The standard Gibbs free energies of denaturation for each domain were determined as functions of pH. These dependences were well approximated by the Harold Scheraga model, which considered the contributions of hydrogen bonds between definite ionogenic groups of a protein to its stability. The number and types of such bonds were determined. These data were generally confirmed by the analysis of the three-dimensional structure of the vicilin molecule.