Proteomics

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Inference and quantification of peptidoforms in large sample cohorts by SWATH-MS: PTM-SWATH-MS Gold Standard data set

ABSTRACT: The PTM-SWATH MS Gold Standard data set consists of a previously published (Soste et al., 2014, PMID:25194849) set of 579 unpurified, synthetic, heavy-isotope labeled phosphopeptides (Thermo Scientific Biopolymers). These phosphopeptides represent biologically relevant sequences from S. cerevisiae proteins, which have been found altered in their phosphorylation status under various conditions. The complete peptide set contains a mixture of singly and doubly phosphorylated sequences with in average more than 3 modifiable residues per peptide (serines, threonines or tyrosins, often in close proximity to each other). All peptides were mixed with equal volumes (concentrations are unknown due to the unpurified status of the peptides) and the resulting peptide mix was either analyzed directly in DDA mode for assay library generation or spiked into a human cell line background proteome in a 13-step dilution series and analyzed in SWATH mode for the generation of the SWATH Gold Standard data set.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Homo Sapiens (human) Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Cell Culture

SUBMITTER: George Rosenberger  

LAB HEAD: Ruedi Aebersold

PROVIDER: PXD004573 | Pride | 2017-06-12

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
20121219_DP_ppeps_plate_mixes_c_75.mzXML.gz Mzxml
20121219_DP_ppeps_plate_mixes_c_76.mzXML.gz Mzxml
20121219_DP_ppeps_plate_mixes_c_77.mzXML.gz Mzxml
20121219_DP_ppeps_plate_mixes_c_81.mzXML.gz Mzxml
20121219_DP_ppeps_plate_mixes_c_82.mzXML.gz Mzxml
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Publications

Consistent detection and quantification of protein post-translational modifications (PTMs) across sample cohorts is a prerequisite for functional analysis of biological processes. Data-independent acquisition (DIA) is a bottom-up mass spectrometry approach that provides complete information on precursor and fragment ions. However, owing to the convoluted structure of DIA data sets, confident, systematic identification and quantification of peptidoforms has remained challenging. Here, we present  ...[more]

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