Download e-book for kindle: Analysis of protein post-translational modifications by mass by John R. Griffiths, Richard D. Unwin

By John R. Griffiths, Richard D. Unwin

ISBN-10: 1119250900

ISBN-13: 9781119250906

  • 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, in addition to key equipment and references
  • Contributions from many of the major researchers within the field
  • A worthy reference resource for all laboratories project 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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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. Genome Biol 2007;8:R250. 15 17 2 Identification and Analysis of Protein Phosphorylation by Mass Spectrometry Dean E. McNulty, Timothy W. Sikorski and Roland S. 1 ­Introduction to Protein Phosphorylation Much of the activity in the cellular proteome is under the control of reversible protein phosphorylation.

To add complexity to this mechanism, under intermediate conditions of phosphate availability, PHO4 is phosphorylated on only one of the sites, allowing it to bind differentially to its target promoters and trigger expression of only a subset of the phosphate-responsive genes [37]. In contrast to PHO4, whose function is regulated by multisite phosphorylation via a single kinase, Sic1 is regulated by a multisite phosphorylation cascade that involves a complex dance of two different kinases. Sic1 controls the G1/S phase transition in budding yeast by inhibiting the S-phase Clb5–Cdk1 kinase.

This mass shift is readily observed on peptides containing the modified amino acid. Thus it was quickly realized that phosphorylated peptides might be readily observed in the FAB spectrum of a protein digest by looking for peptide masses 80 Da (HPO3) higher than predicted. The first reported 25 26 Analysis of Protein Post‐Translational Modifications by Mass Spectrometry analysis of a phosphoprotein by FAB was the identification of a 23-amino acid peptide from chicken egg yolk riboflavin-binding protein that contained eight phosphorylation sites [70].

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


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