Consistency and discrepancy between single molecule force spectroscopy experiments and theoretical models

Single molecule force spectroscopy is a well-established tool to study molecular interactions in a wide range of binding affinities on the single-molecule level. Information about the strength of the molecular bond can be quantified in terms of the dissociation rate k$_{off}$, and the reaction length x$_{b}$ (i.e., the distance between potential minimum and maximum along the direction of pulling). The analysis and interpretation of the underlying force-distance curves is still challenging and various models describing the experimental data are under discussion. In this talk, I will present experimental data for a protein-RNA interaction related to posttranscriptional regulation on the single molecule level, and the interaction between DNA bases forming two or three hydrogen bonds. I will use these examples to discuss the advantages and limitations of this technique, and the consistency and discrepancy to theoretical models.