help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Originally published as Biophys J. BioFAST on September 16, 2005.
doi:10.1529/biophysj.105.067769
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
biophysj.105.067769v1
89/6/4374    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pincet, F.
Right arrow Articles by Husson, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pincet, F.
Right arrow Articles by Husson, J.
Biophysical Journal 89:4374-4381 (2005)
© 2005 The Biophysical Society

The Solution to the Streptavidin-Biotin Paradox: The Influence of History on the Strength of Single Molecular Bonds

Frédéric Pincet and Julien Husson

Laboratoire de Physique Statistique de l'Ecole Normale Supérieure, Paris, France

Correspondence: Address reprint requests to Frédéric Pincet, Laboratoire de Physique Statistique de l'Ecole Normale Supérieure, 24 rue Lhomond, 75231 Paris Cedex 05, France. Tel.: 33-144-32-2502; Fax: 33-144-32-3433; E-mail: pincet{at}lps.ens.fr.

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 reanalyzing 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.




This article has been cited by other articles:


Home page
 Biophys. JHome page
E. B. Walton, S. Lee, and K. J. Van Vliet
Extending Bell's Model: How Force Transducer Stiffness Alters Measured Unbinding Forces and Kinetics of Molecular Complexes
Biophys. J., April 1, 2008; 94(7): 2621 - 2630.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
G. Neuert, C. H. Albrecht, and H. E. Gaub
Predicting the Rupture Probabilities of Molecular Bonds in Series
Biophys. J., August 15, 2007; 93(4): 1215 - 1223.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. Odorico, J.-M. Teulon, T. Bessou, C. Vidaud, L. Bellanger, S.-w. W. Chen, E. Quemeneur, P. Parot, and J.-L. Pellequer
Energy Landscape of Chelated Uranyl: Antibody Interactions by Dynamic Force Spectroscopy
Biophys. J., July 15, 2007; 93(2): 645 - 654.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
N. W. Moore and T. L. Kuhl
The Role of Flexible Tethers in Multiple Ligand-Receptor Bond Formation between Curved Surfaces
Biophys. J., September 1, 2006; 91(5): 1675 - 1687.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. Schlierf and M. Rief
Single-Molecule Unfolding Force Distributions Reveal a Funnel-Shaped Energy Landscape
Biophys. J., February 15, 2006; 90(4): L33 - L35.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2005 by the Biophysical Society.