By John R. Griffiths, Richard D. Unwin
ISBN-10: 1119250900
ISBN-13: 9781119250906
- 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, besides key equipment and references
- Contributions from a few of the best researchers within the field
- A helpful reference resource for all laboratories project proteomics, mass spectrometry and post-translational amendment research
Read Online or Download Analysis of protein post-translational modifications by mass spectrometry PDF
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Extra info for Analysis of protein post-translational modifications by mass spectrometry
Example text
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.
The presence of a doublet with a different intensity ratio followed by a singlet peak 80 Da higher in mass is an indication of a partially phosphorylated peptide. 3c). 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.
In the case of Pho4, it blocks the interaction of Pho4 with nuclear import and export transport proteins and the transcriptional coactivator protein that allows promoter binding. In the case of Sic1, phosphorylation of the priming sites facilitates binding of cyclin/Cdk complexes through their regulatory subunit Cks1. Phosphorylated sites within the three degrons of Sic1 then serve as docking sites for the SCF ubiquitin ligase. 2 Cascades of multisite phosphorylation regulate biological function.
Analysis of protein post-translational modifications by mass spectrometry by John R. Griffiths, Richard D. Unwin
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