Breaking disulfide bonds: β-mercaptoethanol vs. urea
Which reagent breaks disulfide bonds in a protein?
Answer D: explanation for every choice
A
Urea denatures proteins by disrupting hydrogen bonds and hydrophobic interactions, not covalent bonds.
B
SDS is a detergent that denatures by disrupting noncovalent interactions.
C
Trypsin is a protease that cleaves peptide bonds after lysine and arginine.
D
Correct. β-Mercaptoethanol is a reducing agent that converts disulfides back to free thiols.
TakeawayReducing agents (β-mercaptoethanol, DTT) break disulfides. Urea and SDS denature without breaking covalent bonds.
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Reviewed 2026-11-05 by a medical student. Spot an error? Report it with question ID bb24.