Practical Protein Chemistry - A. Darbre 1989

Application of Electron Impact Mass Spectrometry for Determining the Amino Acid Sequence of Peptides and Proteins
Conclusion

Determining the Amino Acid Sequence of Peptides in mixtures using Electron Impact Mass Spectrometry has now become a routine Procedure. Protein chemists equipped with the necessary instrumentation and skilled in mass spectrum interpretation successfully apply mass spectrometry to Complement Other Methods of amino acid sequencing.

The application of mass spectrometry is particularly fruitful in the analysis of poorly separable peptides, peptides with free amide groups, and in determining the Introduction/19.html">Primary Structure of Tryptophan-containing compounds. As a method for amino acid sequencing, mass spectrometry is simply indispensable in the case of peptides with blocked N-termini or those built from Unusual amino acid residues.

In recent years, mass spectrometry with a novel ionization method—fast atom bombardment (FAB) of samples embedded in a glycerol matrix using accelerated inert gas atoms—has come into use for studying non-volatile, polar, and thermally labile compounds [30]. Fast atom bombardment mass spectrometry has been adopted for determining The amino acid sequence of unmodified peptides. It has been reported that under optimal conditions, as little as 15 pmol of peptide is sufficient for this purpose. A more detailed Overview of this novel analytical technique can be found in several specialized papers [31–34].