Local probes of macromolecular structure are measurements that are sensitive to the environment of a relatively small region within a macromolecule. These include, but are not limited to, NMR deuterium exchange and shift perturbation analysis, Fluorescence Resonance Energy Transfer (FRET), and RNA/DNA protein footprinting. The separate transitions reported by individual probes yield unique insight into folding intermediates. While simultaneous acquisition of many unique local transitions provides a cornucopia of information, creating an accurate global description of folding that remains faithful to local details is very challenging.
This software package can be used to analyze such data. Initially, the data is clustered to identify major common transitions. Then, all possible kinetic model topologies are generated and tested to identify the best fitting kinetic model. The software creates a number of graphs and figures to explain the data.