This article is published in Journal of Molecular Recognition as a special issue on Affinity 2009, edited by Gideon Fleminger, Tel-Aviv University, Tel-Aviv, Israel and George Ehrlich, Hoffmann-La Roche, Nutley, NJ, USA.
Force spectroscopy of barnase–barstar single molecule interaction†
Article first published online: 28 OCT 2010
Copyright © 2010 John Wiley & Sons, Ltd.
Journal of Molecular Recognition
Special Issue: Affinity 2009 – The 18th biennial meeting of the International Society for Molecular Recognition
Volume 23, Issue 6, pages 583–588, November/December 2010
How to Cite
Sekatskii, S. K., Favre, M., Dietler, G., Mikhailov, A. G., Klinov, D. V., Lukash, S. V. and Deyev, S. M. (2010), Force spectroscopy of barnase–barstar single molecule interaction. J. Mol. Recognit., 23: 583–588. doi: 10.1002/jmr.1030
- Issue published online: 28 OCT 2010
- Article first published online: 28 OCT 2010
- Manuscript Accepted: 1 FEB 2010
- Manuscript Revised: 8 JAN 2010
- Manuscript Received: 22 SEP 2009
- Swiss National Science Foundation. Grant Number: 200020-119993
- Russian Foundation for Basic Research. Grant Number: 09-04-01201-a
- Russian Federal Agency for Science and Innovation
- ligand-receptor interactions;
- force spectroscopy
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. Copyright © 2010 John Wiley & Sons, Ltd.