Proteomics

Dataset Information

0

Narrow precursor window for DIA-MS enhances protein identification and quantification

ABSTRACT: Data independent acquistion (DIA) is becoming widely as a method of choice in quantitation proteomics due to its high reproducibility and quantitation accuracy at high-throughput fashion. In this project, we systematically evaluated the effect of the selected precursor mass range for DIA-MS on the protein identification and quantification. We show that a narrow precursor window (400-650 m/z) DIA could identify a 34.7% more proteins than a conventional DIA with a wide precursor window of 400-1200 m/z. When combining the three narrow precursor windows (400-650, 650-900, and 900-1200 m/z) DIA-MS analyses, we obtained a 59.4% increase in the number of proteins quantified than a conventional DIA-MS analysis.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Root, Cell Culture

SUBMITTER: Huoming Zhang  

LAB HEAD: Huoming Zhang

PROVIDER: PXD026965 | Pride | 2021-10-01

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
20190701AT_9cell_DIA_400_1000Da_01.raw Raw
20190701AT_9cell_DIA_400_1000Da_01.txt Txt
20190701AT_9cell_DIA_400_1000Da_01_protein_Quant_.xls Xls
20190701AT_9cell_DIA_400_1000Da_02.raw Raw
20190701AT_9cell_DIA_400_1000Da_02.txt Txt
Items per page:
1 - 5 of 126
altmetric image

Publications

Narrow Precursor Mass Range for DIA-MS Enhances Protein Identification and Quantification in Arabidopsis.

Zhang Huoming H   Bensaddek Dalila D  

Life (Basel, Switzerland) 20210918 9

Data independent acquisition-mass spectrometry (DIA-MS) is becoming widely utilised for robust and accurate quantification of samples in quantitative proteomics. Here, we describe the systematic evaluation of the effects of DIA precursor mass range on total protein identification and quantification. We show that a narrow mass range of precursors (~250 m/z) for DIA-MS enables a higher number of protein identifications. Subsequent application of DIA with narrow precursor range (from 400 to 650 m/z  ...[more]

Similar Datasets

Proteomics Systematic Evaluation of Data-Independent Acquisition for Sensitive and Reproducible Proteomics – a Prototype Design for a Single Injection Assay
2015-12-02 | PXD002688 | Pride
Proteomics DIAmeter: Matching peptides to data-independent acquisition mass spectrometry data
2021-05-31 | PXD025385 | Pride
Proteomics DIA+: A novel data-independent acquisition method combines multiple precursor charges to boost peptide signal.
2018-10-11 | PXD010210 | Pride
Proteomics Rapid and in-depth coverage of the (phospho-)proteome with deep libraries and optimal window design for dia-PASEF
2022-08-11 | PXD034128 | Pride
Proteomics Narrow-window DIA: Ultra-fast quantitative analysis of comprehensive proteomes with high sequencing depth. Dilution Series and Single Shot Gradient comparison.
2024-02-01 | PXD046283 | Pride
Proteomics Narrow-window DIA: Ultra-fast quantitative analysis of comprehensive proteomes with high sequencing depth. Evaluation of window width and injection time.
2024-02-01 | PXD046285 | Pride
Proteomics Increasing proteome depth while maintaining quantitative precision in short gradient data-independent acquisition proteomics
2023-05-10 | PXD036451 | Pride
Transcriptomics Expression data from Myotonic dystrophy type 1 (DM1) patient-derived induced pluripotent cell
2024-12-16 | GSE214626 | GEO
Proteomics Gut bacterial phytohormone modulates olfactory sensing, chemotaxis and mortality in fruit fly (Drosophila melanogaster): a new dimension to gut-brain axis
2024-05-22 | PXD044924 | Pride
Proteomics Minute-scale proteomics with Scanning SWATH and high-flow chromatography
2021-03-02 | PXD023613 | Pride