LysC_AHSG_Hec293
Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Others
SUBMITTER: Shabaz Mohammed
PROVIDER: PAe005307 | PeptideAtlas | 2009-12-31
REPOSITORIES: PeptideAtlas
Dataset's files
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Publications
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Gauci Sharon S Helbig Andreas O AO Slijper Monique M Krijgsveld Jeroen J Heck Albert J R AJ Mohammed Shabaz S
Analytical chemistry 20090601 11
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 nonre ...[more]
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