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Disulfide bridges in proteins can be broken by reducing agents, which convert the disulfide bonds (–S–S–) into free thiol groups (–SH). Common reducing agents include dithiothreitol (DTT) and β-mercaptoethanol. The reduction process involves the transfer of electrons to the disulfide bond, leading to its cleavage and the formation of two cysteine residues. This reaction is often performed under controlled conditions to maintain protein structure and function.

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2mo ago

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