Peptide Modifications intermediate
Disulfide Bonds in Peptides: Comprehensive Peptide Reference
Overview of disulfide bond formation between cysteine residues in peptide folding. This modification affects peptide stability, receptor binding, and biologi...
By Encyclopeptide Editorial | 1 min read
disulfide cysteine folding modification
Overview
Disulfide bonds form covalent cross-links between cysteine thiol groups, stabilizing protein tertiary and quaternary structure.
Formation
Catalyzed by protein disulfide isomerase (PDI) in the ER. Ero1 provides oxidizing equivalents.
Patterns
- Intrachain: Stabilize tertiary structure
- Interchain: Link subunits in quaternary structure
- Vicinal: Adjacent cysteines in some toxins
Biological Significance
Disulfide bonds are critical for antibody structure, insulin processing, and extracellular protein stability.
References
- Source: ENCP Peptide Database
- Category: Peptide Modifications
Chemical Identity
| Property | Value |
|---|---|
| Name | Disulfide Bonds in Peptides |
| Category | Peptide Modifications |
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