Read e-book online Analysis of protein post-translational modifications by mass PDF

By John R. Griffiths, Richard D. Unwin

ISBN-10: 1119250900

ISBN-13: 9781119250906

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

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While the data presented earlier would suggest that at least for singly phosphorylated peptides any error resulting from making this assumption is likely to be small, we prefer, in the absence of any empirical evidence, to refer to determinations made in this way as “apparent” stoichiometry. The uncertainty in these apparent stoichiometries is 29 30 Analysis of Protein Post‐Translational Modifications by Mass Spectrometry nevertheless an uncomfortable situation, and so alternative ways to determine phosphorylation occupancy are important to consider.

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 disordered regions contain multiple conserved sequence motifs that serve as docking sites for other proteins, including protein kinases. The flexibility of the disordered regions makes them accessible to PTM, including but not limited to phosphorylation. With the addition of these PTMs, it is estimated that perhaps a million sequence-specific interaction motifs exist with the disordered regions of the proteome [51]. In addition to Sic1, two other well-studied examples of phosphorylation (and other PTM) clusters in disordered regions that control function are p53 [52] and RNA polymerase II [53].

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


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