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Biophys. J. BioFAST: First Published September 16, 2005. doi:10.1529/biophysj.105.067769
© 2005 by the Biophysical Society.


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OTHER

The solution to the streptavidin-biotin paradox: the influence of history on the strength of single molecular bonds

Frederic Pincet 1* and Julien Husson 2

1 LPS-ENS UMR 8550
2 ENS UMR 8550

* To whom correspondence should be addressed. E-mail: pincet{at}lps.ens.fr.

Submitted on June 2, 2005
Revised on July 6, 2005
Accepted on 22 August 2005


   Abstract
In the past few years many studies have attempted to measure the strength of a single molecular bond. In general, these experiments consisted in pulling on the bond and measuring the force necessary to dissociate the molecules. However, seemingly contradictory experimental results led to draw the intriguing conclusion that the strength of the bond could depend on the experiment even if the pulling conditions are similar: this paradox was first observed on the widely used streptavidin-biotin bond. Here, by doing supplementary measurements and by re-analyzing the controversial experimental results using Kramers' theory, we show that they can be conciliated. This allows us to show that the strength of a bond is very sensitive to the history of its formation, which is the key to the paradox.

Key Words: Reaction-rate theory, Streptavidin-biotin, energy landscape, history of a single bond, metastable state




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