  The folding dynamics of proteins at the single molecule level has been
studied with single-molecule force spectroscopy (SMFS) experiments for twenty
years, but a common standardized method for the analysis of the collected data
and for the sharing among the scientific community members is still not
available. We have developed a new open source tool, Fodis, for the analysis of
the Force-distance curves obtained in SMFS experiments, providing an almost
automatic processing, analysis and classification of the obtained data. Our
method provides also a classification of the possible unfolding pathways and
structural heterogeneity, present during the unfolding of proteins.
