Destabilization of VPTANVSVVDLTCR in GAPDH by propachlor exposure may inhibit the active conformation and affect binding partners. No meaningful change in proteolytic susceptibility was observed for IISNASCTNCLAPLAK, which encompasses the propachlor adduct site. Since this peptide can only be observed in GAPDH that has not been directly modified by propachlor, this implies that the stability of unmodified GAPDH is not generally perturbed by the treatment. We also attempted LiP on PARK7 peptides.