ArticleEuropean journal of mass spectrometry (Chichester, England)2015
Native top-down mass spectrometry for the structural characterization of human hemoglobin.
Article in European journal of mass spectrometry (Chichester, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- 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
- A liquid chromatography-high-resolution mass spectrometry method for separation and identification of hemoglobin variant subunits with mass shifts less than 1 Da.Journal of mass spectrometry and advances in the clinical lab · 2025Article
- A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- 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
- Native Top-Down Mass Spectrometry for Characterizing Sarcomeric Proteins Directly from Cardiac Tissue Lysate.Journal of the American Society for Mass Spectrometry · 2024Article
- Probing the functional hotspots inside protein hydrophobic pockets byChemical science · 2024Article
- Miniaturized Raman Instruments for SERS-Based Point-of-Care Testing on Respiratory Viruses.Biosensors · 2022Review
- Fuel source shift or cost reduction: Context-dependent adaptation strategies in closely relatedZoological research · 2022Article
- Structural Biology for the Molecular Insight between Aptamers and Target Proteins.International journal of molecular sciences · 2021Review
- Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry.Chemical science · 2020Review
- Elusive structural changes of New Delhi metallo-β-lactamase revealed by ultraviolet photodissociation mass spectrometry.Chemical science · 2020Article
- Protein Extraction, Enrichment and MALDI MS and MS/MS Analysis from Bitter Orange Leaves (Molecules (Basel, Switzerland) · 2020Article
- Top-Down Characterization of Denatured Proteins and Native Protein Complexes Using Electron Capture Dissociation Implemented within a Modified Ion Mobility-Mass Spectrometer.Analytical chemistry · 2020Article
- Surface-Induced Dissociation: An Effective Method for Characterization of Protein Quaternary Structure.Analytical chemistry · 2019Review
- Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31.Journal of the American Society for Mass Spectrometry · 2019Article
- Radical solutions: Principles and application of electron-based dissociation in mass spectrometry-based analysis of protein structure.Mass spectrometry reviews · 2018Review
- Gas-Phase Protein Salt Bridge Stabilities from Collisional Activation and Electron Transfer Dissociation.International journal of mass spectrometry · 2017Article
- Structural Characterization of a Thrombin-Aptamer Complex by High Resolution Native Top-Down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Top-down/Bottom-up Mass Spectrometry Workflow Using Dissolvable Polyacrylamide Gels.Analytical chemistry · 2017Article
- 193 nm Ultraviolet Photodissociation Mass Spectrometry of Tetrameric Protein Complexes Provides Insight into Quaternary and Secondary Protein Topology.Journal of the American Chemical Society · 2016Article
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Abstract
Native mass spectrometry (MS) has become an invaluable tool for the characterization of proteins and noncovalent protein complexes under near physiological solution conditions. Here we report the structural characterization of human hemoglobin (Hb), a 64 kDa oxygen-transporting protein complex, by high resolution native top-down MS using electrospray ionization and a 15-Tesla Fourier transform ion cyclotron resonance mass spectrometer. Native MS preserves the noncovalent interactions between the globin subunits, and electron capture dissociation (ECD) produces fragments directly from the intact Hb complex without dissociating the subunits. Using activated ion ECD, we observe the gradual unfolding process of the Hb complex in the gas phase. Without protein ion activation, the native Hb shows very limited ECD fragmentation from the N-termini, suggesting a tightly packed structure of the native complex and therefore a low fragmentation efficiency. Precursor ion activation allows a steady increase in N-terminal fragment ions, while the C-terminal fragments remain limited (38 c ions and four z ions on the α chain; 36 c ions and two z ions on the β chain). This ECD fragmentation pattern suggests that upon activation, the Hb complex starts to unfold from the N-termini of both subunits, whereas the C-terminal regions and therefore the potential regions involved in the subunit binding interactions remain intact. ECD-MS of the Hb dimer shows similar fragmentation patterns as the Hb tetramer, providing further evidence for the hypothesized unfolding process of the Hb complex in the gas phase. Native top-down ECD-MS allows efficient probing of the Hb complex structure and the subunit binding interactions in the gas phase. It may provide a fast and effective means to probe the structure of novel protein complexes that are intractable to traditional structural characterization tools.
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