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 variations, together with phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation
  • Discussion of the chemistry in the back of each one amendment, in addition to key equipment and references
  • Contributions from a number of the best researchers within the field
  • A priceless 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

Elias JE, Gygi SP. Target‐decoy search strategy for increased confidence in large‐scale protein identifications by mass spectrometry. Nat Methods 2007;4:207–214. Hornbeck PV, Chabra I, Kornhauser JM, Skrzypek E, Zhang B. PhosphoSite: a bioinformatics resource dedicated to physiological protein phosphorylation. Proteomics 2004;4:1551–1561. Gnad F, Ren S, Cox J, Olsen JV, Macek B, Oroshi M, Mann M. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites.

In addition to the sequence and structural features unique to phosphopeptides, certain sequence features common to all peptides complicate the localization of phosphorylation sites. Very long peptides often suffer from the fact that ions series tend to die out as the collision energy is dissipated over the molecule, leaving large gaps in the sequence information. Tryptic peptides with missed cleavages have internal basic amino acids, which hold a charge firmly and inhibit cleavages based on the mobile proton model of fragmentation.

Thus most phosphopeptides will have more than 33 34 Analysis of Protein Post‐Translational Modifications by Mass Spectrometry one possible location for the phosphorylation to reside. To be certain of the ­phosphorylation site location, an ion series of primary backbone fragments should run across the phosphorylated residue. In practice this is not so easily achieved. Phosphoserine- and phosphothreonine-containing bn and yn ions readily lose phosphate to produce bn-H3PO4 and yn-H3PO4 ions (designated bn▲and yn▲, respectively).

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