Because the HdeA dimer is a partially disordered protein, for which dimer formation and monomer folding occur simultaneously, pulling can be expected to yield multiple pathways along the same reaction coordinate. In general, a one-dimensional reaction coordinate is not a suitable choice for systems where binding is accompanied by large conformational rearrangements. Some success for such systems has been achieved by using the total number of contacts between residues that define the state of the system, as the reaction coordinate, but the analysis of such methods lies beyond the scope of this work.