Force spectroscopy of barnase-barstar single molecule interaction

S. K. Sekatskii, M. Favre, G. Dietler, A. G. Mikhailov, D. V. Klinov, S. V. Lukash, S. M. Deyev

Результат исследований: Материалы для журналаСтатья

10 Цитирования (Scopus)


Results of the single molecule force spectroscopy study of specific interactions between ribonuclease barnase and its inhibitor barstar are presented. Experimental data obtained for the force loading rate ranging 2-70 nN/s are well approximated by a single straight line, from which the dissociation barrier of the width of 0.12 nm and height of 0.75-0.85×10-19 J can be inferred. The measured value of specific interaction does not depend on the NaCl concentration. This apparently contradicts the well-known dependence of the binding energy of this pair on the salt concentration, but such a "contradiction" is explained by the insensitivity of the force spectroscopy data to the relatively long-range electrostatic interaction. The latter essentially contributes to the value of barnase-barstar binding energy revealed by biochemical measurements, and it is exactly this electrostatic interaction which is influenced by the salt concentration.

Язык оригиналаАнглийский
Страницы (с-по)583-588
Число страниц6
ЖурналJournal of Molecular Recognition
Номер выпуска6
СостояниеОпубликовано - ноя 2010
Опубликовано для внешнего пользованияДа

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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  • Цитировать

    Sekatskii, S. K., Favre, M., Dietler, G., Mikhailov, A. G., Klinov, D. V., Lukash, S. V., & Deyev, S. M. (2010). Force spectroscopy of barnase-barstar single molecule interaction. Journal of Molecular Recognition, 23(6), 583-588.