Proteomics

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Comprehensive peptide quantification for data independent acquisition mass spectrometry using chromatogram libraries


ABSTRACT: Raw DDA and DIA data to support Searle et al. 2018. Comprehensive peptide quantification for data independent acquisition mass spectrometry using chromatogram libraries. bioRxiv doi:10.1101/277822

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Saccharomyces Cerevisiae (ncbitaxon:4932)

SUBMITTER: Mike MacCoss   Brian Searle  

PROVIDER: MSV000082805 | MassIVE | Wed Aug 08 20:52:00 BST 2018

REPOSITORIES: MassIVE

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Publications

Chromatogram libraries improve peptide detection and quantification by data independent acquisition mass spectrometry.

Searle Brian C BC   Pino Lindsay K LK   Egertson Jarrett D JD   Ting Ying S YS   Lawrence Robert T RT   MacLean Brendan X BX   Villén Judit J   MacCoss Michael J MJ  

Nature communications 20181203 1


Data independent acquisition (DIA) mass spectrometry is a powerful technique that is improving the reproducibility and throughput of proteomics studies. Here, we introduce an experimental workflow that uses this technique to construct chromatogram libraries that capture fragment ion chromatographic peak shape and retention time for every detectable peptide in a proteomics experiment. These coordinates calibrate protein databases or spectrum libraries to a specific mass spectrometer and chromatog  ...[more]

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