Dataset Information

Trypsin_AHSG_Hec293_r

ABSTRACT: Refined version of low-pH strong cation exchange, Trypsin r2

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Others

SUBMITTER: Shabaz Mohammed

PROVIDER: PAe005308 | PeptideAtlas | 2009-12-31

REPOSITORIES: PeptideAtlas

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			Action	DRS
	PAe005308_10353_tandem.params	Other
	PAe005308_README	Other
	PAe005308_Search_Results_10353_201601070014.properties	Other
	PAe005308_Search_Results_10353_201601070014.tar.gz	Other
	PAe005308_mzXML_201601070009.properties	Other

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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]

PMID: 19413330

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