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

Research output: Contribution to journalArticlepeer-review

10 Citations (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.

Original languageEnglish
Pages (from-to)583-588
Number of pages6
JournalJournal of Molecular Recognition
Issue number6
Publication statusPublished - Nov 2010
Externally publishedYes


  • Barnase
  • Barstar
  • Force spectroscopy
  • Ligand-receptor interactions

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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