ArticleJournal of the American Society for Mass Spectrometry2012
New protein footprinting: fast photochemical iodination combined with top-down and bottom-up mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- FAST MS: Software for the Automated Analysis of Top-Down Mass Spectra of Polymeric Molecules Including RNA, DNA, and Proteins.Journal of the American Society for Mass Spectrometry · 2025Article
- Mass Spectrometry-Based Protein Footprinting for Protein Structure Characterization.Accounts of chemical research · 2025Article
- Covalent Labeling Automated Data Analysis Platform for High Throughput in R (coADAPTr): A Proteome-Wide Data Analysis Platform for Covalent Labeling Experiments.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
- Isotopic Depletion Increases the Spatial Resolution of FPOP Top-Down Mass Spectrometry Analysis.Analytical chemistry · 2024Article
- Precursor Reagent Hydrophobicity Affects Membrane Protein Footprinting.Journal of the American Society for Mass Spectrometry · 2023Article
- Top-Down Proteoform Analysis by 2D MS with Quadrupolar Detection.Analytical chemistry · 2023Article
- Top-Down Detection of Oxidative Protein Footprinting by Collision-Induced Dissociation, Electron-Transfer Dissociation, and Electron-Capture Dissociation.Analytical chemistry · 2022Article
- Multiplex Chemical Labeling of Amino Acids for Protein Footprinting Structure Assessment.Analytical chemistry · 2022Article
- Characterizing Endogenous Protein Complexes with Biological Mass Spectrometry.Chemical reviews · 2022Review
- Carbocation Footprinting of Soluble and Transmembrane Proteins.Analytical chemistry · 2021Article
- THE MAKING OF A FOOTPRINT IN PROTEIN FOOTPRINTING: A REVIEW IN HONOR OF MICHAEL L. GROSS.Mass spectrometry reviews · 2021Review
- Free-Radical Membrane Protein Footprinting by Photolysis of Perfluoroisopropyl Iodide Partitioned to Detergent Micelle by Sonication.Angewandte Chemie (International ed. in English) · 2021Article
- Protein higher-order-structure determination by fast photochemical oxidation of proteins and mass spectrometry analysis.Nature protocols · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Fast Protein Footprinting by X-ray Mediated Radical Trifluoromethylation.Journal of the American Society for Mass Spectrometry · 2020Article
- The Application of Fluorine-Containing Reagents in Structural Proteomics.Angewandte Chemie (International ed. in English) · 2020Review
- Fast photochemical oxidation of proteins (FPOP): A powerful mass spectrometry-based structural proteomics tool.The Journal of biological chemistry · 2019Review
- Protein-Metal-Ion Interactions Studied by Mass Spectrometry-Based Footprinting with Isotope-Encoded Benzhydrazide.Analytical chemistry · 2019Article
- Implementing fast photochemical oxidation of proteins (FPOP) as a footprinting approach to solve diverse problems in structural biology.Methods (San Diego, Calif.) · 2018Review
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Authors and funding
4 authors.
Funding
Abstract
We report a new approach for the fast photochemical oxidation of proteins (FPOP) whereby iodine species are used as the modifying reagent. We generate the radicals by photolysis of iodobenzoic acid at 248 nm; the putative iodine radical then rapidly modifies the target protein. This iodine-radical labeling is sensitive, tunable, and site-specific, modifying only histidine and tyrosine residues in contrast to OH radicals that modify 14 amino-acid side chains. We iodinated myoglobin (Mb) and apomyoglobin (aMb) in their native states and analyzed the outcome by both top-down and bottom-up proteomic strategies. Top-down sequencing selects a certain level (addition of one I, two I's) of modification and determines the major components produced in the modification reaction, whereas bottom-up reveals details for each modification site. Tyr146 is found to be modified for aMb but less so for Mb. His82, His93, and His97 are at least 10 times more modified for aMb than for Mb, in agreement with NMR studies. For carbonic anhydrase and its apo form, there are no significant differences of the modification extents, indicating their similarity in conformation and providing a control for this approach. For lispro insulin, insulin-EDTA, and insulin complexed with zinc, iodination yields are sensitive to differences in insulin oligomerization state. The iodine radical labeling is a promising addition to protein footprinting methods, offering higher specificity and lower reactivity than ∙OH and SO(4)(-∙), two other radicals already employed in FPOP.
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