Which outcome decreases catalytic activity when cysteine residues form disulfide bonds?

💡 Explanation

When cysteine forms disulfide bonds, intramolecular cross-linking causes conformational strain because local structure changes distort three-dimensional shape impacting protein folding near active site essential for catalysis. Therefore decreased activity results, rather than increased affinity, enhanced interactions, or resistance to denaturation that require correct conformation.

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