Phosphoproteomics

Phosphoproteomics is the study of protein phosphorylation, which is one of the most studied and important posttranslational modifications (PTM) in proteins. It can be found on residues of serine, threonine, and tyrosine. Many biological activities, including cell cycle progression, proliferation, and apoptosis, are regulated by this PTM. Ion-exchange chromatography is used to separate the peptides. To compensate for the low abundance of phosphopeptides, a last step of phosphopeptide enrichment is performed before mass spectrometry analysis. In phosphoproteomics, many phosphopeptide enrichment approaches are used. Immunoprecipitation can be utilized for phosphopeptide enrichment in circumstances when a single phosphorylated amino acid is being sought. Antibodies produced against phosphorylated amino acids are used to bind and isolate the peptide in this method. It's more difficult to identify and quantify phosphopeptide sites than it is to measure non-phosphorylated proteins. Because phosphorylation is a dynamic and error-prone process, some protein phosphorylation events occur without significant functional significance. Because of the high sensitivity of contemporary mass spectrometers, random phosphorylation events will be detected while examining vast amounts of proteins.