How can a two-carbon molecule help scientists take a huge protein apart?
2-Mercaptoethanol reduces disulfide bonds—the covalent S-S bridges that can stabilize a protein or connect separate protein chains.
This is why it is commonly used in reducing protein electrophoresis. Detergent and heat disrupt many noncovalent interactions, while 2-mercaptoethanol tackles the disulfide bonds that may remain.
Break those sulfur bridges, and individual polypeptide chains can separate and unfold more completely.
HOCH2CH2SH is tiny compared with a protein, but its thiol group gives it the chemistry needed to undo some of the protein's strongest structural connections.
Global Chemical Database