Introduction AFM probes can be transformed into sensitive, chemically selective biosensors by attaching ligand molecules to the tips of the probes. Single-molecule molecular recognition force microscopy (MRFM) is an AFM-based technique that relies heavily on probes that have been modifi ed with ligand molecules [Riener et al. 2003, Hinterdorfer 2004]. In MRFM, single-molecule unbinding interactions between ligands and complementary receptors that are immobilized on a substrate are observed and quantifi ed one by one as the AFM cantilever approaches and subsequently withdraws from the substrate. These force spectroscopy (FS) experiments can provide valuable information about the structure and dynamics of molecular unbinding events at the single-molecule level [Noy et al. 1997]. The technique has also been effectively applied to gain an understanding of the intramolecular forces involved in protein folding and polymer elongation [Allison et al. 2002].