Analysis of protein post-translational modifications by mass by John R. Griffiths, Richard D. Unwin

By John R. Griffiths, Richard D. Unwin

  • Covers all significant transformations, together with phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation
  • Discussion of the chemistry at the back of each one amendment, in addition to key tools and references
  • Contributions from a few of the prime researchers within the field
  • A worthwhile reference resource for all laboratories project proteomics, mass spectrometry and post-translational amendment research

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Additional info for Analysis of protein post-translational modifications by mass spectrometry

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An extensive primary y ion series from y1 to y14 indicates that there is no phosphorylation on the four possibilities in the C-terminus. A single N-terminal fragment, represented by an unmodified b2 ion, suggests that the phosphate is on S3. With no other supporting evidence, point mutants were made for each the first three amino acids, and phosphorylation exclusively on S3 was confirmed using an in vivo activity assay [109]. The ability of MS/MS to localize sites of phosphorylation may be further compromised by the recent evidence that in the gas phase, phosphate groups can migrate to other hydroxyl-containing amino acids [110, 111].

It is still a requirement that the peptides are pure or the final determination of the absolute stoichiometry will be no more certain than the apparent stoichiometry. Clearly this approach does not scale well as the number of sites to be determined increases. Nor is it always possible to synthesize peptides for certain long or multiply phosphorylated species that are unstable over time. As an alternative, our laboratory described an approach that uses phosphatase digestion and differential chemical labeling to determine absolute stoichiometry [101].

The first evidence that kinases worked in series came in 1968 with the discovery of cAMP-dependent protein kinase A (PKA) and the fact that it phosphorylated and activated phosphorylase kinase [13]. It quickly became clear that PKA had many substrates in multiple tissues [14], and the idea that protein phosphorylation was a widespread phenomenon began to take hold. Throughout the 1970s and 1980s many additional serine/threonine (S/T) protein kinases were discovered, and in 1983 Tony Hunter showed that the v-Src protein was a tyrosine kinase (TK) [15].

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