Proteomics

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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

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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
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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]

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