ArticleAnalytical chemistry2017
Variable-Velocity Traveling-Wave Ion Mobility Separation Enhancing Peak Capacity for Data-Independent Acquisition Proteomics.
Article in Analytical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
- High-Throughput Screening of Isomeric Reaction Products by Droplet Microfluidics Coupled to Cyclic Ion Mobility-Mass Spectrometry.Analytical chemistry · 2026Article
- Gas-phase unfolding assay rapidly predicts structure-function relationships in engineered antibodies with tuned flexibilities.Nature communications · 2026Article
- Article
- Assessment of Variable Traveling Wave Profiles for Small-Molecule Applications in Ion Mobility Spectrometry-Mass Spectrometry (IMS-MS).Journal of the American Society for Mass Spectrometry · 2025Article
- High-Throughput Monoclonal Antibody Peptide Mapping Using 15-s HPLC Gradients Coupled with Cyclic Ion Mobility-Mass Spectrometry.Analytical chemistry · 2025Article
- Experimental Evidence for Phosphorylation-Driven Allosteric Regulation of Alpha Synuclein Function.bioRxiv : the preprint server for biology · 2025Article
- Ion Mobility-Assisted Free Radical-Initiated Peptide Sequencing.International journal of mass spectrometry · 2025Article
- Improved Annotation of Internal Fragments via Trapped-Ion Mobility Enhanced Top-Down Sequencing of Protein Ions.Journal of mass spectrometry : JMS · 2025Article
- A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Native ion mobility-mass spectrometry reveals the binding mechanisms of anti-amyloid therapeutic antibodies.Protein science : a publication of the Protein Society · 2024Article
- Triboelectric Nanogenerators for the Masses: A Low-Cost Do-It-Yourself Pulsed Ion Source for Sample-Limited Applications.Journal of the American Society for Mass Spectrometry · 2024Article
- Cyclic Ion Mobility-Mass Spectrometry and Tandem Collision Induced Unfolding for Quantification of Elusive Protein Biomarkers.Analytical chemistry · 2024Article
- Application of Ion Mobility Spectrometry and the Derived Collision Cross Section in the Analysis of Environmental Organic Micropollutants.Environmental science & technology · 2023Review
- Uncovering DUB Selectivity through an Ion Mobility-Based Assessment of Ubiquitin Chain Isomers.Analytical chemistry · 2023Article
- Collision Induced Unfolding Enables the Quantitation of Isomass Biotherapeutics in Complex Biological Matrices.Journal of the American Society for Mass Spectrometry · 2023Article
- Oxidized and Reduced Dimeric Protein Complexes Illustrate Contrasting CID and SID Charge Partitioning.Journal of the American Society for Mass Spectrometry · 2023Article
- Resolving Hidden Solution Conformations of Hemoglobin Using IMS-IMS on a Cyclic Instrument.Journal of the American Society for Mass Spectrometry · 2023Article
- Quantitative Analysis of Diubiquitin Isomers Using Ion Mobility Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2023Article
- Hydrogen/deuterium exchange-mass spectrometry of integral membrane proteins in native-like environments: current scenario and the way forward.Essays in biochemistry · 2023Article
- Intrinsically disordered interaction network in an RNA chaperone revealed by native mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
High mass accuracy, data-dependent acquisition is the current standard method in mass spectrometry-based peptide annotation and quantification. In high complexity samples, limited instrument scan speeds often result in under-sampling. In contrast, all-ion data-independent acquisition methods bypass precursor selection, alternating high and low collision energies to analyze product and precursor ions across wide mass ranges. Despite capturing data for all events, peptide annotation is limited by inadequate alignment algorithms or overlapping ions. Ion mobility separation can add an orthogonal analytical dimension, reducing ion interference to improve reproducibility, peak capacity, and peptide identifications to rival modern hybrid quadrupole orbitrap systems. Despite the advantages of ion mobility separation in complex proteomics analyses, there has been no quantitative measure of ion mobility resolution in a complex proteomic sample. Here, we present TWIMExtract, a data extraction tool to export defined slices of liquid chromatography/ion mobility/mass spectrometry (LC-IM-MS) data, providing a route to quantify ion mobility resolution from a commercial traveling-wave ion mobility time-of-flight mass spectrometer. Using standard traveling-wave ion mobility parameters (600 m/s, 40 V), 90% of the annotated peptides occupied just 23% of the ion mobility drift space, yet inclusion of ion mobility nearly doubled the overall peak capacity. Relative to fixed velocity traveling-wave ion mobility settings, ramping the traveling-wave velocity increased drift space occupancy, amplifying resolution by 16%, peak capacity by nearly 50%, and peptide/protein identifications by 40%. Overall, variable-velocity traveling-wave ion mobility-mass spectrometry significantly enhances proteomics analysis in all-ion fragmentation acquisition.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.