Answer:
Disulfide linkage/bond
Explanation:
The tertiary and quarternary structure of the protein is stabilized by Disulfide linkage which is formed between two thiol groups in the protein. 2-mercaptoethanol is a reducing agent that breaks this disulfide bond.
A protein becomes denature when it loses its native configuration and becomes inactive. So as 2-mercaptoethanol breaks disulfide bond in protein it looses its native configuration and becomes denatured. 2-mercaptoethanol is used in SDS-PAGE to separate protein subunits. Therefore the correct answer is Disulfide linkage/bond.
It makes the proteins ................
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