The sequence of amino acids in a protein or peptide can be identified by Edman degradation, which was developed by Pehr Edman. This method can label and cleave the peptide from N-terminal without disrupting the peptide bonds between other amino acid residues.
2. Developed by Pehr Edman, is a method of sequencing
amino acids in a peptide
The Edman degradation reaction was automated in 1967
by Edman and Beggs to speed up the process. Now,
automated Edman sequencers are used widely, and it can
sequence peptides up to approximately 50 amino acids.
The amino acid of N-terminal residue is labeled and cleaved
from the peptide without disrupting the peptide bonds
between other amino acid residues.
5. Applications
Verification of the N-terminal
boundary of recombinant
proteins or determination the N-
terminus of protease-resistant
domains
Identify proteins as to some novel
proteins and peptides where sequence
databases are not available for MS/MS
database searching
Identify the new N-terminal
and proteolytic cleavage site in
the protein fragments
6. Advantages and disadvantages
2
2
1
4
1
3
Identify the exact N-
terminal amino acid
The released amino acids
are identified and quantified
by chromatography.
Enable N-terminal
sequencing of proteins in
mixtures
It will not work if the N-terminus
has been chemically modified
Sequencing will stop if a non-α-
amino acid is encountered
Edman degradation is generally
not useful to determine the
positions of disulfide bridges
3
Larger proteins cannot be
sequenced by the Edman
sequencing
7. Our Services
At Creative, we can provide N-terminal sequence analysis by both Edman and Mass spectrometry of
therapeutic proteins, monoclonal antibodies and protein vaccines. In our view, Edman sequencing and
mass spectrometric analysis provide complementary information.
Sequence Analysis of Peptides or Proteins
8. Thank You
Please contact us for more information
Web
Email
www.creative-proteomics.com
info@creative-proteomics.com
We are looking forward to cooperating with you.