Dynamic force spectroscopy: optimized data analysis

The forced rupture of single chemical bonds in biomolecular compounds (e.g., ligand-receptor systems) as observed in dynamic force spectroscopy experiments is addressed. An optimized method of data analysis is proposed. This method significantly outperforms the current standard one when applied to data from an idealized numerical computer simulation of an experiment with realistic parameter values. In particular, the force-free dissociation rate can be inferred with a considerably smaller statistical uncertainty and without the systematic overestimation of about 30%, which is shown to be inherent in the standard method.