Disulfide bond
A covalent bond formed between two cysteine residues in a peptide chain. Disulfide bonds stabilize three-dimensional structure and are critical for the biological activity of many peptides including insulin.
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Related Terms
The overall three-dimensional shape of a folded peptide or protein, determined by interactions between side chains including disulfide bonds, hydrophobic interactions, and ionic bonds.
StabilityA peptide’s resistance to chemical degradation over time. Affected by temperature, pH, light, and oxidation. Lyophilized peptides are most stable; reconstituted peptides should be refrigerated and used within 28 days.
CyclizationThe process of forming a ring structure within a peptide chain, typically through disulfide bonds or amide bonds between the N- and C-termini. Cyclization increases stability, receptor selectivity, and resistance to enzymatic degradation.