Visual CyclicCyclization Chemistry
Cyclic peptides are formed by covalently linking backbone or side-chain residues. Visual Cyclic supports calculation and visualization for common cyclization strategies.
Head-to-tail cyclization
The N-terminus is linked to the C-terminus to form a backbone macrocycle. This results in a mass loss (loss of H₂O for peptide bond). The Cyclization Mass Shift tool computes the mass change and resulting molecular weight.
Cyclization Mass Shift →Disulfide bonds
Cysteine residues can form disulfide bonds (S–S), cyclizing the peptide or stabilizing a folded structure. The mass change is −2 Da per disulfide (loss of two H). Use the 3D Viewer and Disulfide Bond 3D to visualize disulfide connectivity.
Disulfide Bond 3D →Other cyclization
Thioether (e.g. cysteine–maleimide), lactam (side-chain to backbone), and other linkers are used in cyclic and stapled peptides. Molecular weight and stability depend on the chemistry. Use Cyclic Peptide Properties for sequence-based properties and the Stability Predictor for stability indices.
Using Visual Cyclic
Enter cyclic peptide sequence in Cyclic Peptide Properties for cyclization loss, pI, MW, and disulfide bonds. Use the Stability Predictor for stability indices and the 3D viewer for structure. Data sources include CyBase, ConoServer, PDB, and UniProt.
Data Sources (CyclicPepedia) · Cyclic Structure Export · Docs