Lysine Propionylation Boosts Proteome Sequence Coverage and Enables a “Silent SILAC” Labeling Strategy for Relative Protein Quantification
Schräder, C.U.; Moore, S.; Goodarzi, A.A.; et al.
Quantitative proteomic protocols incorporating stable isotopes tend to do so with metabolic or chemical processes and typically utilize trypsin. Although the utility of alternative proteases has been demonstrated, quantitative studies using these alternatives are effectively non-existent. Here, Schriemer and colleagues developed a novel isotope labeling strategy to quantify metabolically labeled proteins on the MS2 level regardless of protease. This relies on SILAC-like metabolic labeling and TMT-like quantitative analysis, to deliver improved protein sequence coverage without sacrifice to protein identifications.
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