Which type of bond stabilizes tertiary structure between cysteine residues?

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Multiple Choice

Which type of bond stabilizes tertiary structure between cysteine residues?

Disulfide bonds form covalent links between the sulfur atoms of cysteine residues, creating crosslinks that lock distant parts of a protein together and stabilize its three-dimensional shape. These S-S bonds arise when cysteine thiol groups are oxidized to form cystine, and they can link segments within a single chain or connect different chains. This covalent crosslink is stronger and more enduring than non-covalent interactions like salt bridges or hydrogen bonds, which help shape the fold but don’t provide a permanent crosslink between cysteines. Peptide bonds, meanwhile, connect amino acids in the primary sequence, not the tertiary stabilization between cysteine residues.

Disulfide bonds form covalent links between the sulfur atoms of cysteine residues, creating crosslinks that lock distant parts of a protein together and stabilize its three-dimensional shape. These S-S bonds arise when cysteine thiol groups are oxidized to form cystine, and they can link segments within a single chain or connect different chains. This covalent crosslink is stronger and more enduring than non-covalent interactions like salt bridges or hydrogen bonds, which help shape the fold but don’t provide a permanent crosslink between cysteines. Peptide bonds, meanwhile, connect amino acids in the primary sequence, not the tertiary stabilization between cysteine residues.

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