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 | |
| 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
Force spectroscopy of barnase-barstar single molecule interaction. / Sekatskii, S. K.; Favre, M.; Dietler, G.; Mikhailov, A. G.; Klinov, D. V.; Lukash, S. V.; Deyev, S. M.
In: Journal of Molecular Recognition, Vol. 23, No. 6, 11.2010, p. 583-588.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Force spectroscopy of barnase-barstar single molecule interaction
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
Y1 - 2010/11
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
UR - http://www.scopus.com/inward/record.url?scp=78049450703&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=78049450703&partnerID=8YFLogxK
U2 - 10.1002/jmr.1030
DO - 10.1002/jmr.1030
M3 - Article
AN - SCOPUS:78049450703
VL - 23
SP - 583
EP - 588
JO - Journal of Molecular Recognition
JF - Journal of Molecular Recognition
SN - 0952-3499
IS - 6
ER -