  We probe the dynamic strength of multiple biotin-streptavidin adhesion bonds
under linear loading using the biomembrane force probe setup for dynamic force
spectroscopy. Measured rupture force histograms are compared to results from a
master equation model for the stochastic dynamics of bond rupture under load.
This allows us to extract the distribution of the number of initially closed
bonds. We also extract the molecular parameters of the adhesion bonds, in good
agreement with earlier results from single bond experiments. Our analysis shows
that the peaks in the measured histograms are not simple multiples of the
single bond values, but follow from a superposition procedure which generates
different peak positions.
