ArticleAnalytical chemistry2021
Surface-Induced Dissociation of Protein Complexes Selected by Trapped Ion Mobility Spectrometry.
Article in Analytical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Adapting a Trapped Ion Mobility Spectrometry-Q-TOF for HighAnalytical chemistry · 2025Article
- Evaluation of a Commercial TIMS-Q-TOF Platform for Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Laser capture microdissection and native mass spectrometry for spatially-resolved analysis of intact protein assemblies in tissue.Chemical science · 2024Article
- Enhancing the Depth of Analyses with Next-Generation Ion Mobility Experiments.Annual review of analytical chemistry (Palo Alto, Calif.) · 2023Review
- Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section.Chemical reviews · 2023Review
- Matrix-Landing Mass Spectrometry for Electron Microscopy Imaging of Native Protein Complexes.Analytical chemistry · 2022Article
- Trapped Ion Mobility Spectrometry, Ultraviolet Photodissociation, and Time-of-Flight Mass Spectrometry for Gas-Phase Peptide Isobars/Isomers/Conformers Discrimination.Journal of the American Society for Mass Spectrometry · 2022Article
- Tandem-trapped ion mobility spectrometry/mass spectrometry (The Analyst · 2022Review
- Native Mass Spectrometry: Recent Progress and Remaining Challenges.Annual review of biophysics · 2022Review
- Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.Chemical reviews · 2022Review
- Surface-induced dissociation of protein complexes on a cyclic ion mobility spectrometer.The Analyst · 2021Article
- 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
6 authors at 2 institutions in 1 country.
Funding
Abstract
Native mass spectrometry (nMS), particularly in conjunction with gas-phase ion mobility spectrometry measurements, has proven useful as a structural biology tool for evaluating the stoichiometry, conformation, and topology of protein complexes. Here, we demonstrate the combination of trapped ion mobility spectrometry (TIMS) and surface-induced dissociation (SID) on a Bruker SolariX XR 15 T FT-ICR mass spectrometer for the structural analysis of protein complexes. We successfully performed SID on mobility-selected protein complexes, including the streptavidin tetramer and cholera toxin B with bound ligands. Additionally, TIMS-SID was employed on a mixture of the peptides desArg1 and desArg9 bradykinin to mobility-separate and identify the individual peptides. Importantly, results show that native-like conformations can be maintained throughout the TIMS analysis. The TIMS-SID spectra are analogous to SID spectra acquired using quadrupole mass selection, indicating little measurable, if any, structural rearrangement during mobility selection. Mobility parking was used on the ion or mobility of interest and 50-200 SID mass spectra were averaged. High-quality TIMS-SID spectra were acquired over a period of 2-10 min, comparable to or slightly longer than SID coupled with ion mobility on various instrument platforms in our laboratory. The ultrahigh resolving power of the 15 T FT-ICR allowed for the identification and relative quantification of overlapping SID fragments with the same nominal
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Registered trials
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