ArticleAnalytical chemistry2022
Tandem Trapped Ion Mobility Spectrometry/Mass Spectrometry (tTIMS/MS) Reveals Sequence-Specific Determinants of Top-Down Protein Fragment Ion Cross Sections.
Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Disambiguation of Product Ion Assignments, Including Internal Fragment Ions from Top-Down Mass Spectrometry, Using Ion Mobility-Aligned Fragmentation (MAF).Analytical chemistry · 2026Article
- Time-Resolved Study of In Situ Generated Protein Subcomplexes by Tandem-Trapped Ion Mobility Spectrometry.Journal of mass spectrometry : JMS · 2026Article
- Development and Modification of Ion Mobility Mass Spectrometry Instrumentation for Enhanced Analysis of Biological Molecules.Journal of the American Society for Mass Spectrometry · 2025Review
- Differential melting voltage by tandem-trapped ion mobility spectrometry: glycan structure influences glycoprotein stability.RSC chemical biology · 2025Article
- A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- The path forward for protein footprinting, covalent labeling, and mass spectrometry-based protein conformational analyses.Journal of mass spectrometry : JMS · 2024Review
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Metastability of Protein Solution Structures in the Absence of a Solvent: Rugged Energy Landscape and Glass-like Behavior.Journal of the American Chemical Society · 2024Article
- Peptide collision cross sections of 22 post-translational modifications.Analytical and bioanalytical chemistry · 2023Article
- Elucidating Structures of Protein Complexes by Collision-Induced Dissociation at Elevated Gas Pressures.Journal of the American Society for Mass Spectrometry · 2023Article
- Top-Down Protein Analysis by Tandem-Trapped Ion Mobility Spectrometry/Mass Spectrometry (Tandem-TIMS/MS) Coupled with Ultraviolet Photodissociation (UVPD) and Parallel Accumulation/Serial Fragmentation (PASEF) MS/MS Analysis.Journal of the American Society for Mass Spectrometry · 2023Article
- Article
- Enhancing the Depth of Analyses with Next-Generation Ion Mobility Experiments.Annual review of analytical chemistry (Palo Alto, Calif.) · 2023Review
- Characterizing the top-down sequencing of protein ions prior to mobility separation in a timsTOF.The Analyst · 2023Article
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Authors and funding
6 authors.
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Abstract
Top-down proteomics provides a straightforward approach to the level of proteoforms but remains technologically challenging. Using ion mobility spectrometry/mass spectrometry (IMS/MS) to separate top-down fragment ions improves signal/noise and dynamic range. Such applications, however, do not yet leverage the primary information obtained from IMS/MS, which is the characterization of the fragment ion structure by the measured momentum transfer cross sections. Here, we perform top-down analysis of intact proteins and assemblies using our tandem trapped ion mobility spectrometer/mass spectrometer (tTIMS/MS) and compile over 1400 cross section values of fragment ions. Our analysis reveals that most fragment ions exhibit multiple, stable conformations similar to those of intact polypeptides and proteins. The data further indicate that the conformational heterogeneity is strongly influenced by the amino acid sequences of the fragment ions. Moreover, time-resolved tTIMS/MS experiments reveal that conformations of top-down fragment ions can be metastable on the timescale of ion mobility measurements. Taken together, our analysis indicates that top-down fragment ions undergo a folding process in the gas phase and that this folding process can lead to kinetic trapping of intermediate states in ion mobility measurements. Hence, because the folding free energy surface of a polypeptide ion is encoded by its amino acid sequence and charge state, our analysis suggests that cross sections can be exploited as sequence-specific determinants of top-down fragment ions.
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