Abstract
Mass spectrometry (MS) has now become the method of choice for identifying posttranslational modifications in proteins, for protein mapping studies and for some aspects of protein sequence analysis. In the early 1980s, two major advances in mass spectrometry combined to allow its more widespread application to protein analysis. These were the development of high-field magnet instrumentation (1), in the mid-70s, allowing routine high-mass applications for the first time; and, subsequently, the introduction of the fastatom bombardment (FAB) technique in 1981 (2). FAB-MS enabled previously intractable, thermally labile, and highly polar compounds such as peptides, to be analyzed with minimal sample preparation and no chemical derivatization. Since then, methods and instrumentation for characterizing protein and carbohydrate structure by MS have advanced rapidly. These developments were complemented in the late 1980s with the introduction of electrospray (ES-MS) ionization (3,4), allowing the analysis of very large molecules on conventional mass range instruments.
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References
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Greer, F.M., Morris, H.R. (1997). Fast-Atom Bombardment and Electrospray Mass Spectrometry of Peptides, Proteins, and Glycoproteins. In: Smith, B.J. (eds) Protein Sequencing Protocols. Methods in Molecular Biology™, vol 64. Humana Press, Totowa, NJ. https://doi.org/10.1385/0-89603-353-8:147
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DOI: https://doi.org/10.1385/0-89603-353-8:147
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