ArticleAnalytical chemistry2014
Fragmentation of integral membrane proteins in the gas phase.
Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Native Top-Down Analysis of Membrane Protein Complexes Directly From In Vitro and Native Membranes.Molecular & cellular proteomics : MCP · 2025Article
- Capillary Zone Electrophoresis-Mass Spectrometry of Intact G Protein-Coupled Receptors Enables Proteoform Profiling.Analytical chemistry · 2025Article
- Top-down mass spectrometry of native proteoforms and their complexes: a community study.Nature methods · 2024Article
- Mass spectrometry-intensive top-down proteomics: an update on technology advancements and biomedical applications.Analytical methods : advancing methods and applications · 2024Review
- Top-down proteomics.Nature reviews. Methods primers · 2024Article
- Nonionic, Cleavable Surfactant for Top-Down Proteomics.Analytical chemistry · 2023Article
- Novel Strategies to Address the Challenges in Top-Down Proteomics.Journal of the American Society for Mass Spectrometry · 2021Review
- Top-Down Proteomics of Endogenous Membrane Proteins Enabled by Cloud Point Enrichment and Multidimensional Liquid Chromatography-Mass Spectrometry.Analytical chemistry · 2020Article
- Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry.Chemical science · 2020Review
- Enhanced Characterization of Membrane Protein Complexes by Ultraviolet Photodissociation Mass Spectrometry.Analytical chemistry · 2020Article
- Recent advances in mass spectrometry based clinical proteomics: applications to cancer research.Clinical proteomics · 2020Review
- Towards mapping electrostatic interactions between KdoThe Analyst · 2018Article
- The Value of Activated Ion Electron Transfer Dissociation for High-Throughput Top-Down Characterization of Intact Proteins.Analytical chemistry · 2018Article
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- Top-Down Proteomics: Ready for Prime Time?Analytical chemistry · 2018Review
- Integral membrane proteins: bottom-up, top-down and structural proteomics.Expert review of proteomics · 2017Review
- Ion Activation Methods for Peptides and Proteins.Analytical chemistry · 2016Review
- Top-down mass spectrometry of intact membrane protein complexes reveals oligomeric state and sequence information in a single experiment.Protein science : a publication of the Protein Society · 2015Article
- Mass spectrometric analysis of the cell surface N-glycoproteome by combining metabolic labeling and click chemistry.Journal of the American Society for Mass Spectrometry · 2015Article
- Structural characterization of holo- and apo-myoglobin in the gas phase by ultraviolet photodissociation mass spectrometry.Chemical science · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Integral membrane proteins (IMPs) are of great biophysical and clinical interest because of the key role they play in many cellular processes. Here, a comprehensive top down study of 152 IMPs and 277 soluble proteins from human H1299 cells including 11 087 fragments obtained from collisionally activated dissociation (CAD), 6452 from higher-energy collisional dissociation (HCD), and 2981 from electron transfer dissociation (ETD) shows their great utility and complementarity for the identification and characterization of IMPs. A central finding is that ETD is ∼2-fold more likely to cleave in soluble regions than threshold fragmentation methods, whereas the reverse is observed in transmembrane domains with an observed ∼4-fold bias toward CAD and HCD. The location of charges just prior to dissociation is consistent with this directed fragmentation: protons remain localized on basic residues during ETD but easily mobilize along the backbone during collisional activation. The fragmentation driven by these protons, which is most often observed in transmembrane domains, both is of higher yield and occurs over a greater number of backbone cleavage sites. Further, while threshold dissociation events in transmembrane domains are on average 10.1 (CAD) and 9.2 (HCD) residues distant from the nearest charge site (R, K, H, N-terminus), fragmentation is strongly influenced by the N- or C-terminal position relative to that site: the ratio of observed b- to y-fragments is ∼1:3 if the cleavage occurs >7 residues N-terminal and ∼3:1 if it occurs >7 residues C-terminal to the nearest basic site. Threshold dissociation products driven by a mobilized proton appear to be strongly dependent on not only relative position of a charge site but also N- or C-terminal directionality of proton movement.
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Registered trials
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