---
title: "Edman degradation Template – Chemistry Diagram | MolDraw"
url: https://www.moldraw.com/templates/edman-degradation/
description: "Edman degradation template: The N-terminal amine adds to phenyl isothiocyanate to give the PTC-peptide; in anhydrous TFA the thiocarbonyl S attacks the first…"
lang: en
publisher: Scidart Academy
generated: 2026-11-13
---
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# Edman degradation template

![Edman degradation template: The N-terminal amine adds to phenyl isothiocyanate to give the PTC-peptide; in anhydrous TFA the thiocarbonyl S attacks the first peptide C=O and the shortened peptide leaves as an amine, giving the anilinothiazolinone (ATZ), which aqueous acid converts to the PTH-amino acid.](https://www.moldraw.com/templates/edman-degradation.webp)

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The N-terminal amine adds to phenyl isothiocyanate to give the PTC-peptide; in anhydrous TFA the thiocarbonyl S attacks the first peptide C=O and the shortened peptide leaves as an amine, giving the anilinothiazolinone (ATZ), which aqueous acid converts to the PTH-amino acid.

## Mechanism step by step

PITC tags the N-terminal residue; anhydrous acid cuts it off as a thiazolinone and leaves the rest of the chain intact

1. **Coupling (pH 9)** – The free α-NH₂ adds to the N=C=S carbon
2. **Proton transfer** – The phenylthiocarbamoyl (PTC) peptide
3. **Protonation (TFA)** – Anhydrous acid protonates the first peptide C=O
4. **Cyclisation** – Sulfur bonds to the activated carbonyl carbon (5-membered ring); the anilino N takes the positive charge
5. **Proton transfer** – H⁺ moves from O to the next residue’s N (via the solvent)
6. **Peptide leaves** – C=O reforms and the shortened peptide departs as a neutral amine
7. **Deprotonation** – The anilinothiazolinone (ATZ), extracted into organic solvent
8. **Conversion** – Aqueous acid opens the ATZ and recloses it to the stable PTH-amino acid

## Key points

- Coupling needs the free, unprotonated α-NH₂ (pH 8–9); the cleavage is done in anhydrous acid so that no other peptide bond is hydrolysed.
- Only the first residue is removed. The shortened peptide goes round the cycle again, one residue per cycle, read by HPLC of the PTH-amino acids.
- Repetitive yields of about 99% limit a run to roughly 30–50 residues; longer proteins are cut into fragments first, and a blocked N-terminus stops it.
- Unlike Sanger’s FDNB method, Edman degradation does not destroy the rest of the chain. Edman and Begg automated it in the sequenator (1967).

Drawn with 312 atoms, 25 arrows, 12 shapes – every one editable in MolDraw.

## Sources

- [Nelson & Cox, Lehninger Principles of Biochemistry, 8th ed., 2021, ch. 3](https://openlibrary.org/isbn/9781319228002) Textbook
- [Berg, Tymoczko, Gatto & Stryer, Biochemistry, 9th ed., 2019](https://openlibrary.org/isbn/9781319114657) Textbook
- [Edman, Arch. Biochem. 1949, 22, 475](https://pubmed.ncbi.nlm.nih.gov/18134557/) Original paper
- [Edman & Begg, Eur. J. Biochem. 1967, 1, 80](https://pubmed.ncbi.nlm.nih.gov/6059350/) Original paper

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## Frequently asked questions

### Is the Edman degradation template free?

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