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.
North atlantic and the pacific by japan
I would answer that as Answer D) Checking it’s conductivity
Pretty sure it’s all of the above
In The metabolism of amino acids for energy, what is the fate of the amino group?
Excreted as urea