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Post-translational modification

Post-translational modifications constitute a key mechanism for influencing the properties of many proteins, such as turnover rate, localization and interactions. The modifications can be introduced into, and removed from, proteins in a very rapid manner to affect protein function. Most studies of the effect and the roles of PTMs have focused on the analysis of a fairly small number of PTMs. The analysis of protein modification and has been greatly facilitated by key developments in peptide fractionation using column-based chromatography and affinity matrices able to pull down modified peptides in batch formats from complex mixtures.

Modified peptides can be considerably enriched compared to non-modified peptides for example, on the basis of charge (by ion‑exchange (IEX) chromatography, such as strong anion exchange), hydrophilic interaction liquid chromatography (HILIC) or of metal-based affinity methods. 

Phosphopeptide enrichment is critical for two primary reasons: phosphopeptides exist at low stoichiometric abundances and they can be suppressed during ionization. Enrichment strategies have, and continue to, evolve with variations on loading, column format, and elution conditions. See the protocol section for our TiO2 strategy.

Glycopeptide enrichment is essential for site-specific glycosylation analysis using MS due to the presence of sub-stoichiometric levels of individual glycopeptides that result from glycosylation heterogeneity. Several methods have been developed to enrich glycopeptides prior to analysis and they have different specificity or selectivity depending on the type of glycosylation to study. Enquire the facility for expertise in this field.

Page Manager: Jörgen Bergström|Last update: 3/29/2016
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