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Identifying an Abnormal Phosphorylated Adaptor by Viral Kinase Using Mass Spectrometry.

Chenhe SuChenhao SuChunfu Zheng
Published in: Methods in molecular biology (Clifton, N.J.) (2024)
Mass spectrometers are widely used to identify protein phosphorylation sites. The process usually involves selective isolation of phosphoproteins and subsequent fragmentation to identify both the peptide sequence and phosphorylation site. Immunoprecipitation could capture and purify the protein of interest, greatly reducing sample complexity before submitting it for mass spectrometry analysis. This chapter describes a method to identify an abnormal phosphorylated site of the adaptor protein by a viral kinase through immunoprecipitation followed by LC-MS/MS.
Keyphrases
  • mass spectrometry
  • protein kinase
  • protein protein
  • amino acid
  • sars cov
  • liquid chromatography
  • high resolution
  • binding protein
  • capillary electrophoresis
  • high performance liquid chromatography
  • small molecule