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

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Abstract

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 language	English
Pages (from-to)	583-588
Number of pages	6
Journal	Journal of Molecular Recognition
Volume	23
Issue number	6
DOIs	https://doi.org/10.1002/jmr.1030
Publication status	Published - Nov 2010
Externally published	Yes

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Keywords

Barnase
Barstar
Force spectroscopy
Ligand-receptor interactions

ASJC Scopus subject areas

Molecular Biology
Structural Biology

Cite this

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. https://doi.org/10.1002/jmr.1030

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abstract = "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.",

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author = "Sekatskii, {S. K.} and M. Favre and G. Dietler and Mikhailov, {A. G.} and Klinov, {D. V.} and Lukash, {S. V.} and Deyev, {S. M.}",

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AU - Sekatskii, S. K.

AU - Favre, M.

AU - Dietler, G.

AU - Mikhailov, A. G.

AU - Klinov, D. V.

AU - Lukash, S. V.

AU - Deyev, S. M.

PY - 2010/11

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N2 - 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.

AB - 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.

KW - Barnase

KW - Barstar

KW - Force spectroscopy

KW - Ligand-receptor interactions

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Access to Document

10.1002/jmr.1030