Abstract
The rapid developments in the field of mass spectrometry have transformed it into a key technology in proteome research.
Increased sensitivity in mass spectrometry, as a result of more efficient ionisation techniques and better detectors, has allowed the stepwise reduction of protein quantity for analysis. Protein spots of 2D-PAGE separated samples are now quantitatively sufficient for an unequivocal identification of a protein by mass spectrometry. In addition to protein identification a closer look at posttranslational modifications is now also possible. It is speculated that modifications like phosphorylation or glycosylation exist on every second protein and that they are important for the protein function.
This review highlights the different mass spectrometric methods and gives a brief overview of strategies and methods used to identify modifications.
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Sickmann, A., Mreyen, M., Meyer, H.E. (2003). Mass Spectrometry — a Key Technology in Proteom Research. In: Hecker, M., et al. Proteomics of Microorganisms. Advances in Biochemical Engineering/Biotechnology, vol 83. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-36459-5_6
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DOI: https://doi.org/10.1007/3-540-36459-5_6
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