<unk> , developed by Pehr<unk> , is a method of sequencing amino acids in a peptide. In this method, the amino-terminal residue is labeled and cleaved from the peptide without disrupting the peptide bonds between other amino acid residues.
Phenylisothiocyanate is reacted with an uncharged terminal amino group, under mildly alkaline conditions, to form a phenylthiocarbamoyl derivative. Then, under acidic conditions, this derivative of the terminal amino acid is cleaved as a thiazolinone derivative. The thiazolinone amino acid is then selectively extracted into an organic solvent and treated with acid to form the more stable phenylthiohydantoin (PTH)- amino acid derivative that can be identified by using chromatography or electrophoresis. This procedure can then be repeated again to identify the next amino acid. A major drawback to this technique is that the peptides being sequenced in this manner cannot have more than 50 to 60 residues. This is because the<unk>  reaction is not 100% efficient, meaning that the cleavage step does not occur every time. However, this problem can be resolved by cleaving large peptides into smaller peptides before proceeding with the reaction. It is able to accurately sequence up to 30 amino acids with 98% efficiency per amino acid. An advantage of the<unk>  is that it only uses 10 - 100 picomoles of peptide for the sequencing process.<unk>  reaction is automated to speed up the process.
Edman degradation
Bergmann degradation
Fischer esterification
Beta oxidation
Glucuronidation
Biotinylation
Hydrogen-deuterium exchange
Chiral pool synthesis