Proteins use disulfide (SS) bonds as “pillars” contributes higher conformational stability. Heat-induced SS bond breakages inside protein molecules generate highly reactive perthiole (R-SSH) that triggers SS-shuffling chain-reaction for irreversible denaturation.
We found this chain-reaction can be suppressed by adding methanethiosulfonate (MTS) type reagents that quickly eliminate perthiol groups, which are the starting point of the reaction. This methodology is now trying to medical applications.