Refined procedure of evaluating experimental single-molecule force spectroscopy data

Alexander Fuhrmann, Dario Anselmetti, Robert Ros, Sebastian Getfert, Peter Reimann

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


Dynamic force spectroscopy is a well-established tool to study molecular recognition in a wide range of binding affinities on the single-molecule level. The theoretical interpretation of these data is still very challenging and the models describe the experimental data only partly. In this paper we reconsider the basic assumptions of the models on the basis of an experimental data set and propose an approach of analyzing and quantitatively evaluating dynamic force spectroscopy data on single ligand-receptor complexes. We present our procedure to process and analyze the force-distance curves, to detect the rupture events in an automated manner, and to calculate quantitative parameters for a biophysical characterization of the investigated interaction.

Original languageEnglish (US)
Article number031912
JournalPhysical Review E - Statistical, Nonlinear, and Soft Matter Physics
Issue number3
StatePublished - Mar 13 2008
Externally publishedYes

ASJC Scopus subject areas

  • Statistical and Nonlinear Physics
  • Statistics and Probability
  • Condensed Matter Physics


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