Force spectroscopy of barnase-barstar single molecule interaction

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

Keywords

Barnase
Barstar
Force spectroscopy
Ligand-receptor interactions

ASJC Scopus subject areas

Molecular Biology
Structural Biology

Access to Document

10.1002/jmr.1030

Fingerprint Dive into the research topics of 'Force spectroscopy of barnase-barstar single molecule interaction'. Together they form a unique fingerprint.

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

@article{fb94ae87838b403194c07cd84c3b247b,

title = "Force spectroscopy of barnase-barstar single molecule interaction",

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.",

keywords = "Barnase, Barstar, Force spectroscopy, Ligand-receptor interactions",

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.}",

year = "2010",

month = nov,

doi = "10.1002/jmr.1030",

language = "English",

volume = "23",

pages = "583--588",

journal = "Journal of Molecular Recognition",

issn = "0952-3499",

publisher = "John Wiley and Sons Ltd",

number = "6",

}

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 -