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 alterations, together with phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation
  • Discussion of the chemistry at the back of each one amendment, besides key equipment and references
  • Contributions from a few of the prime researchers within the field
  • A worthwhile 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

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Unwin. © 2017 John Wiley & Sons, Inc. Published 2017 by John Wiley & Sons, Inc. 18 Analysis of Protein Post‐Translational Modifications by Mass Spectrometry phosphate was on the amino acid serine [7], it was not until 1932 that Levene and Fritz Lipmann isolated phosphoserine from vitellin [8]. Prior to the 1950s, research on phosphoproteins was focused mainly on abundant proteins found in egg yolk (such as vitellin) and milk (casein), and the biological function, if any, of the phosphorylation was unknown.

B) Partial ES mass spectrum of a sample containing a phosphorylated (○) peptide and its nonphosphorylated counterpart (●). The apparent stoichiometry determined from this spectrum is 31%. (c) After being taken through the protocol, each peptide adds one propionyl group, either d0 or d5. The absolute stoichiometry determined from the nonphosphorylated d0/d5 cluster is 45%. See text for details. of the phosphorylated peptide. The stoichiometry (S) is determined from the intensities of the nonphosphorylated pair using the equation S = 1 − (IL/IH), where IL is the intensity of the untreated sample tagged with the light label (L) and IH is the intensity of phosphatase-treated sample tagged with the heavy label (H).

Intrinsically disordered proteins (IDP) play a central role in mediating protein–protein interactions and the assembly of complex protein interaction networks [50]. 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].

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