DC Biosciences PTM service enables you to answer questions about the post-translational modifications on your proteins.
Post-translational modifications (PTMs) on proteins are an often understudied and neglected area of proteomics. Yet, PTMs have a huge impact on the cellular function of proteins.
The diversity and relatively low-abundance of modified peptides compared to the unmodified counterparts complicates the study of PTMs. The detection and identification of PTMs by LC-MSMS can be improved by selectively enriching for modified peptides/proteins using a variety of methods (affinity resins, antibodies, etc.). The PTM-enriched fraction is then analysed separately from the non-enriched sample.
Subsequent analysis of the data obtained by mass spectrometry and comparison with the specific protein database must also take into account the PTM. Including too many modifications in a search, however, can increase the likelihood of a false match. Therefore, it is important to carefully think about the PTMs you are interested in and to apply the appropriate enrichment approach.
The most commonly-studied PTMs are phosphorylation, ubiquitination (and modification by ubiquitin-like proteins) and glycosylation. Other PTMs, such as acetylation, methylation, and hydroxylation, are emerging as new research foci.