Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

@article{Gauci2009LysNAT,
  title={Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.},
  author={Sharon Gauci and Andreas O. Helbig and Monique Slijper and Jeroen Krijgsveld and Albert J. R. Heck and Shabaz Mohammed},
  journal={Analytical chemistry},
  year={2009},
  volume={81 11},
  pages={4493-501}
}
The analysis of proteome-wide phosphorylation events is still a major analytical challenge because of the enormous complexity of protein phosphorylation networks. In this work, we evaluate the complementarity of Lys-N, Lys-C, and trypsin with regard to their ability to contribute to the global analysis of the phosphoproteome. A refined version of low-pH strong cation exchange was used to efficiently separate N-terminally acetylated, phosphorylated, and nonmodified peptides. A total of 5036… CONTINUE READING

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