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Originally published as Biophys J. BioFAST on March 2, 2006.
doi:10.1529/biophysj.105.077099
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Biophysical Journal 90:3851-3864 (2006)
© 2006 The Biophysical Society

Theoretical Analysis of Single-Molecule Force Spectroscopy Experiments: Heterogeneity of Chemical Bonds

M. Raible *, M. Evstigneev *, F. W. Bartels {dagger}, R. Eckel {dagger}, M. Nguyen-Duong {ddagger}, R. Merkel {ddagger}, R. Ros {dagger}, D. Anselmetti {dagger} and P. Reimann *

* Theoretische Physik, and {dagger} Experimentelle Biophysik, Universität Bielefeld, Bielefeld, Germany; and {ddagger} Institute of Thin Films and Interfaces, Research Centre Jülich, Jülich, Germany

Correspondence: Address reprint requests to Mykhaylo Evstigneev, E-mail: mykhaylo{at}physik.uni-bielefeld.de.

We show that the standard theoretical framework in single-molecule force spectroscopy has to be extended 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.




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