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Sulfhydryl group-containing proteins are proteins that possess one or more sulfhydryl (–SH) groups, primarily in the side chains of cysteine residues. These –SH groups, also known as thiols, play critical roles in protein structure and function, including disulfide bond formation, catalysis, redox regulation, and detoxification. Glutathione is a prominent example. Their reactivity makes them targets for both therapeutic intervention and toxicological insult.
Modulation of protein function via thiol modification (oxidation, alkylation, metal binding). Glutathione acts as a direct antioxidant by scavenging free radicals and detoxifying xenobiotics.
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