ArticleChemical science2019
Expanding the mass range for UVPD-based native top-down mass spectrometry.
Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- A Prototype timsOmni Platform Enables Confident Annotation of the Key Hypervariable CDR3 Regions of IgG Immunoglobulins Using Low- and High-Energy Electron-Based Fragmentation.Analytical chemistry · 2026Article
- On the Utility of Infrared Photoactivation for Native Top-Down and Complex-Down Orbitrap Mass Spectrometry of Soluble Proteoform Complexes.Journal of the American Society for Mass Spectrometry · 2026Article
- Structural mass spectrometry techniques for characterisation of plant and algal proteins.The Plant journal : for cell and molecular biology · 2026Review
- How to Use Quantum Chemistry for Analyzing Mass Spectrometry Data.Mass spectrometry (Tokyo, Japan) · 2026Review
- Top-Down Proteomics for the Characterization and Quantification of Calreticulin Arginylation.Analytical chemistry · 2025Article
- Defining proteoform-specific interactions for drug targeting in a native cell signalling environment.Nature chemistry · 2025Article
- Top-down Proteomics for the Characterization and Quantification of Calreticulin Arginylation.bioRxiv : the preprint server for biology · 2024Article
- [Applications of native mass spectrometry and ultraviolet photodissociation in protein structure and interaction analysis].Se pu = Chinese journal of chromatography · 2024Review
- Tracking Inhibition of Human Small C-Terminal Domain Phosphatase 1 Using 193 nm Ultraviolet Photodissociation Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Instrumentation at the Leading Edge of Proteomics.Analytical chemistry · 2024Review
- Laser capture microdissection and native mass spectrometry for spatially-resolved analysis of intact protein assemblies in tissue.Chemical science · 2024Article
- Infrared Photoactivation Enables Improved Native Top-Down Mass Spectrometry of Transmembrane Proteins.Analytical chemistry · 2023Article
- An Orbitrap/Time-of-Flight Mass Spectrometer for Photofragment Ion Imaging and High-Resolution Mass Analysis of Native Macromolecular Assemblies.Journal of the American Society for Mass Spectrometry · 2023Article
- Nonionic, Cleavable Surfactant for Top-Down Proteomics.Analytical chemistry · 2023Article
- High-Resolution Native Mass Spectrometry.Chemical reviews · 2022Review
- Recent technological developments for native mass spectrometry.Biochimica et biophysica acta. Proteins and proteomics · 2022Review
- Extending Native Top-Down Electron Capture Dissociation to MDa Immunoglobulin Complexes Provides Useful Sequence Tags Covering Their Critical Variable Complementarity-Determining Regions.Analytical chemistry · 2021Article
- The lysosomal endopeptidases Cathepsin D and L are selective and effective proteases for the middle-down characterization of antibodies.The FEBS journal · 2021Article
- Reassembling protein complexes after controlled disassembly by top-down mass spectrometry in native mode.International journal of mass spectrometry · 2021Article
- Evolution of a virus-like architecture and packaging mechanism in a repurposed bacterial protein.Science (New York, N.Y.) · 2021Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Native top-down mass spectrometry is emerging as a methodology that can be used to structurally investigate protein assemblies. To extend the possibilities of native top-down mass spectrometry to larger and more heterogeneous biomolecular assemblies, advances in both the mass analyzer and applied fragmentation techniques are still essential. Here, we explore ultraviolet photodissociation (UVPD) of protein assemblies on an Orbitrap with extended mass range, expanding its usage to large and heterogeneous macromolecular complexes, reaching masses above 1 million Da. We demonstrate that UVPD can lead not only to the ejection of intact subunits directly from such large intact complexes, but also to backbone fragmentation of these subunits, providing enough sequence information for subunit identification. The Orbitrap mass analyzer enables simultaneous monitoring of the precursor, the subunits, and the subunit fragments formed upon UVPD activation. While only partial sequence coverage of the subunits is observed, the UVPD data yields information about the localization of chromophores covalently attached to the subunits of the light harvesting complex B-phycoerythrin, extensive backbone fragmentation in a subunit of a CRISPR-Cas Csy (type I-F Cascade) complex, and sequence modifications in a virus-like proteinaceous nano-container. Through these multiple applications we demonstrate for the first time that UVPD based native top-down mass spectrometry is feasible for large and heterogeneous particles, including ribonucleoprotein complexes and MDa virus-like particles.
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