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Biophys. J. BioFAST: First Published March 2, 2006. doi:10.1529/biophysj.105.077099
© 2006 by the Biophysical Society.

A more recent version of this article appeared on June 1, 2006.
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BIOPHYSICAL THEORY AND MODELING

Theoretical analysis of single-molecule force spectroscopy experiments: heterogeneity of chemical bonds

Martin Raible 1, Mykhaylo Evstigneev 2*, Frank W. Bartels 3, Rainer Eckel 3, M. Nguyen-Duong 4, Rudolf Merkel 4, Robert Ros 3, Dario Anselmetti 3 and Peter Reimann 2

1 Theoretische Physik, Universitaet Bielefeld, Germany
2 Theoretische Physik, Universitaet Bielefeld
3 Experimentelle Biophysik, Universitaet Bielefeld
4 Institute of Thin Films and Interfaces, Research Centre Juelich

* To whom correspondence should be addressed. E-mail: mykhaylo{at}physik.uni-bielefeld.de.

Submitted on November 2, 2005
Revised on December 19, 2005
Accepted on 25 January 2006


  Abstract
We show that the standard theoretical framework in single-molecule force spectroscopy by Evans and Ritchie [Biophys. J. 72, 1541 (1997)] has to be extended in order to consistently describe the experimental findings. The basic amendment is to take into account heterogeneity of the chemical bonds via random variations of the force dependent dissociation rates. This results in a very good agreement between theory and rupture data from several different experiments.

Key Words: Chemical reaction kinetics, Single molecule force spectroscopy




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Copyright © 2006 by the Biophysical Society.