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

By John R. Griffiths, Richard D. Unwin

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

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

Example text

As might be expected, a weak but significant correlation exists between a protein’s abundance and the number of sites identified in an analysis [5]. However, it is clear that multisite phosphorylation is the rule rather than the exception. It has been suggested that the multiplicity of phosphorylation on proteins might just be background noise. However, it is equally likely that given the wide variety of biological functions under the control of protein phosphorylation and the wide variety of mechanisms by which it occurs, the functional significance of most of the complex hyperphosphorylation that occurs on proteins is not yet understood.

A complicating issue in this approach is the recent evidence that what appear to be M-H3PO4 ions might actually derive from the loss of HPO3 (-80) followed by the simultaneous loss of H20 (-18) from a nearby serine or threonine [110]. In this case, the MS3 spectrum of an M-98 ion would be incorrectly interpreted. The actual phosphoserine residue would have the in-chain mass of an unmodified serine, and the actual unmodified serine would have the in-chain mass of dehydroalanine. Even more complicating would be the situation where the M-98 ion was a mixture of M-H3PO4 and M-HPO3 followed by M-H2O.

31. The phosphorylated (○) and nonphosphorylated (●) peptide pair give rise to three peaks. 31 arises from the half of the sample that was treated with alkaline phosphatase. It represents the total amount of the sequence present in that half of the sample (sum of phosphopeptide and nonphosphopeptide). 81 comes from the half of the sample that was not treated with phosphatase, and it thus represents the original amount of nonphosphorylated peptide. 3 Determination of absolute stoichiometry. (a) Schematic showing the generalized protocol.

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