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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry.

In the context of proteome analysis, matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) can fulfil the two tasks of primary structure verification and protein identification. As an illustration of the first of these tasks, the sequence of Eschericha coli isoleucyl-tRNA synthetase, a protein with 15 reported sequence conflicts, has been established by means of MALDI mass mapping. The identification of mitochondrial proteins participating in a yeast supramolecular complex exhibiting NADH dehydrogenase activity highlights the performances of MALDI-MS for the second task. The spectral suppression phenomenon occurring for complex peptide mixtures analysed by MALDI is discussed, as well as the role of post-source decay analysis for confident protein identification.[1]

References

  1. Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry. Belghazi, M., Bathany, K., Hountondji, C., Grandier-Vazeille, X., Manon, S., Schmitter, J.M. Proteomics (2001) [Pubmed]
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