Protein kinase A phosphorylation characterized by tandem Fourier transform ion cyclotron resonance mass spectrometry.

@article{Chalmers2004ProteinKA,
  title={Protein kinase A phosphorylation characterized by tandem Fourier transform ion cyclotron resonance mass spectrometry.},
  author={Michael J. Chalmers and Kristina H{\aa}kansson and Robert B. Johnson and Richard Smith and Jianwei J Shen and Mark R. Emmett and Alan G. Marshall},
  journal={Proteomics},
  year={2004},
  volume={4 4},
  pages={970-81}
}
A microelectrospray ionization tandem Fourier transform ion cyclotron resonance mass spectrometry (ESI FT-ICR MS(n)) approach for structural characterization of protein phosphorylation is described. Identification of proteolytic peptides is based solely upon mass measurement by high field (9.4 Tesla) FT-ICR MS. The location of the modification within any phosphopeptide is then established by FT-ICR MS(2) and MS(3) experiments. Structural information is maximized by use of electron capture… CONTINUE READING

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