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Protein enrichment is a technique by which proteins of a particular type in a biological sample are concentrated for further analysis and identification. Enrichment is used to help concentrate low-abundance proteins to improve their downstream analysis.
Enrichment of biotinylated peptides using an anti-biotin antibody results in substantially improved biotinylation site identifications by mass spectrometry compared to traditional streptavidin-based biotinylated protein enrichment.
Capture of low-abundance multiply phosphorylated peptides (MPPs) is difficult due to limitation of enrichment materials and their interactions with phosphates. Here the authors show, a smart polymer driven by specific but tunable hydrogen bonding interactions can differentially complex with MPPs, singly phosphorylated and non-modified peptides.
This protocol enables the study of protein complexes by trapping them in virus-like particles and thereby preserving cellular integrity. The Virotrap protocol is complemented by SFINX, an online data analysis tool for interactomics studies.