Proteomics

Dataset Information

0

Trypsin_AHSG_Hec293


ABSTRACT: Refined version of low-pH strong cation exchange, Trypsin r1

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Others

SUBMITTER: Shabaz Mohammed 

PROVIDER: PAe005306 | PeptideAtlas | 2009-12-31

REPOSITORIES: PeptideAtlas

Dataset's files

Source:
Action DRS
PAe005306_10351_tandem.params Other
PAe005306_README Other
PAe005306_Search_Results_10351_201601070007.properties Other
PAe005306_Search_Results_10351_201601070007.tar.gz Other
PAe005306_mzXML_201601070001.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]

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