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Reversible protein phosphorylation ranks among the most important post-translational modifications that occurs in the cell. It is therefore highly relevant to elucidate the phosphorylation states of a given biological system, albeit challenging. Most notably the often low stoichiometry of phosphorylation is inherently incompatible with standard LC-MS analysis of a complex protein digest mixture, primarily due to the relative low dynamic range of current mass analyzers. Therefore a need for specific enrichment of phosphorylated peptides or proteins exists. Significant progress surrounding the biochemical analysis of reversible protein phosphorylation in the past years has led to the development of several new techniques to isolate or enrich phosphopeptides, particularly in large-scale analyses. This chapter deals with three such examples.
|Item Type:||Journal Article, refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > Functional Genomics Center Zurich|
07 Faculty of Science > Institute of Molecular Life Sciences
|DDC:||570 Life sciences; biology|
610 Medicine & health
|Deposited On:||04 Jun 2012 14:10|
|Last Modified:||27 Nov 2013 21:27|
|Citations:||Web of Science®. Times Cited: 1|
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