By John R. Griffiths, Richard D. Unwin
- Covers all significant changes, together with phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation
- Discussion of the chemistry at the back of every one amendment, in addition to key equipment and references
- Contributions from the various top researchers within the field
- A precious reference resource for all laboratories project proteomics, mass spectrometry and post-translational amendment research
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Covers all significant changes, together with phosphorylation, glycosylation, acetylation, ubiquitination, sulfonation and and glycation dialogue of the chemistry in the back of each one amendment, in addition to key equipment and references Contributions from a number of the top researchers within the box A important reference resource for all laboratories venture proteomics, mass spectrometry and post-translational amendment examine
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Extra resources for Analysis of protein post-translational modifications by mass spectrometry
Although the spectrum is not dominated by the neutral loss of phosphate from the precursor, the abundant loss of H3PO4 from fragment ions makes localization of the sites difficult; however there is evidence for the localization as shown. See the text for details. (b) CID spectrum of a singly phosphorylated peptide assigned to the sequence TSSIADEGTYTLDSILR. The doubly charged precursor was fragmented using low-energy CID on a quadrupole time-of-flight hybrid. Notice the residual unfragmented precursor (marked •).
In contrast, a separate study examining 66 model peptides and their singly phosphorylated counterparts found that in nearly all cases the phosphopeptides had lower ionization efficiency than their nonphosphorylated counterparts . But here again, the average difference in relative ionization efficiency was only a factor of two. In this study three sets of peptides were created based on a single sequence and all contained a C-terminal Lys residue. The charge and hydrophobicity in each set were varied by making fixed substitutions at specific sites within the sequence.
The main advantages of the MSA acquisition over an MS3 acquisition are that they take much less time, that they result in only a single spectrum, and that the signal-to-noise ratio of MSA spectra is much better. The value of performing either MS3 or MSA is debatable. For proteome-scale studies it is not clear that the impact on the duty cycle of the experiment is offset by an increase in phosphopeptide identifications. The evidence in the literature is quite conflicting [113, 116–119]. The assumption is that while fewer spectra are acquired, the quality of these spectra will result in more identifications.