ArticleMass spectrometry (Tokyo, Japan)2021
Effect of Phosphorylation on the Collision Cross Sections of Peptide Ions in Ion Mobility Spectrometry.
Article in Mass spectrometry (Tokyo, Japan), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Studying Mucin-Derived O-Glycopeptides with Gas-Phase FRET.Analytical chemistry · 2026Article
- Leveraging pretrained deep protein language model to predict peptide collision cross section.Communications chemistry · 2025Article
- Thunder-DDA-PASEF enables high-coverage immunopeptidomics and is boosted by MSNature communications · 2024Article
- Peptide collision cross sections of 22 post-translational modifications.Analytical and bioanalytical chemistry · 2023Article
- Considerations for defining +80 Da mass shifts in mass spectrometry-based proteomics: phosphorylation and beyond.Chemical communications (Cambridge, England) · 2023Review
- Ionmob: a Python package for prediction of peptide collisional cross-section values.Bioinformatics (Oxford, England) · 2023Article
- Rapid and In-Depth Coverage of the (Phospho-)Proteome With Deep Libraries and Optimal Window Design for dia-PASEF.Molecular & cellular proteomics : MCP · 2022Article
- Trapped Ion Mobility Spectrometry and Parallel Accumulation-Serial Fragmentation in Proteomics.Molecular & cellular proteomics : MCP · 2021Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The insertion of ion mobility spectrometry (IMS) between LC and MS can improve peptide identification in both proteomics and phosphoproteomics by providing structural information that is complementary to LC and MS, because IMS separates ions on the basis of differences in their shapes and charge states. However, it is necessary to know how phosphate groups affect the peptide collision cross sections (CCS) in order to accurately predict phosphopeptide CCS values and to maximize the usefulness of IMS. In this work, we systematically characterized the CCS values of 4,433 pairs of mono-phosphopeptide and corresponding unphosphorylated peptide ions using trapped ion mobility spectrometry (TIMS). Nearly one-third of the mono-phosphopeptide ions evaluated here showed smaller CCS values than their unphosphorylated counterparts, even though phosphorylation results in a mass increase of 80 Da. Significant changes of CCS upon phosphorylation occurred mainly in structurally extended peptides with large numbers of basic groups, possibly reflecting intramolecular interactions between phosphate and basic groups.
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