Evaluation of irreversible protein thermal inactivation caused by breakage of disulphide bonds using methanethiosulphonate.

ABSTRACT: Many extracellular globular proteins have evolved to possess disulphide bonds in their native conformations, which aids in thermodynamic stabilisation. However, disulphide bond breakage by heating leads to irreversible protein denaturation through disulphide-thiol exchange reactions. In this study, we demonstrate that methanethiosulphonate (MTS) specifically suppresses the heat-induced disulphide-thiol exchange reaction, thus improving the heat-resistance of proteins. In the presence of MTS, small globular proteins that contain disulphides can spontaneously refold from heat-denatured states, maintaining wild-type disulphide pairing. Because the disulphide-thiol exchange reaction is triggered by the generation of catalytic amounts of perthiol or thiol, rapid and specific perthiol/thiol prot

SUBMITTER: Futami J 

PROVIDER: S-EPMC5622167 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature