ArticleMethods (San Diego, Calif.)2015
Using hydroxyl radical footprinting to explore the free energy landscape of protein folding.
Article in Methods (San Diego, Calif.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed.
- Nafamostat Mesylate Regulates Glycosylation to Alleviate Aristolochic Acid Induced Kidney Injury.Toxins · 2025Article
- Review
- Investigation of D76N βJournal of the American Society for Mass Spectrometry · 2021Article
- In Vivo Proton Exchange Rate (kJournal of magnetic resonance imaging : JMRI · 2021Article
- PyXlinkViewer: A flexible tool for visualization of protein chemical crosslinking data within the PyMOL molecular graphics system.Protein science : a publication of the Protein Society · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Rapid Quantification of Peptide Oxidation Isomers From Complex Mixtures.Analytical chemistry · 2020Article
- Hydroxyl-Radical Reaction Pathways for the Fast Photochemical Oxidation of Proteins Platform As Revealed byAnalytical chemistry · 2019Article
- Comparing Hydrogen Deuterium Exchange and Fast Photochemical Oxidation of Proteins: a Structural Characterisation of Wild-Type and ΔN6 βJournal of the American Society for Mass Spectrometry · 2018Article
- Conformational flexibility within the nascent polypeptide-associated complex enables its interactions with structurally diverse client proteins.The Journal of biological chemistry · 2018Article
- Imaging short-lived reactive oxygen species (ROS) with endogenous contrast MRI.Journal of magnetic resonance imaging : JMRI · 2018Article
- Topological Dissection of the Membrane Transport Protein Mhp1 Derived from Cysteine Accessibility and Mass Spectrometry.Analytical chemistry · 2017Article
- Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment.Molecular & cellular proteomics : MCP · 2017Review
- FPOP-LC-MS/MS Suggests Differences in Interaction Sites of Amphipols and Detergents with Outer Membrane Proteins.Journal of the American Society for Mass Spectrometry · 2017Article
- Carbene footprinting accurately maps binding sites in protein-ligand and protein-protein interactions.Nature communications · 2016Article
- Probing the Time Scale of FPOP (Fast Photochemical Oxidation of Proteins): Radical Reactions Extend Over Tens of Milliseconds.Journal of the American Society for Mass Spectrometry · 2016Article
- Meandering Down the Energy Landscape of Protein Folding: Are We There Yet?Biophysical journal · 2016Review
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Authors and funding
4 authors.
Funding
Abstract
Characterisation of the conformational states adopted during protein folding, including globally unfolded/disordered structures and partially folded intermediate species, is vital to gain fundamental insights into how a protein folds. In this work we employ fast photochemical oxidation of proteins (FPOP) to map the structural changes that occur in the folding of the four-helical bacterial immunity protein, Im7. Oxidative footprinting coupled with mass spectrometry (MS) is used to probe changes in the solvent accessibility of amino acid side-chains concurrent with the folding process, by quantifying the degree of oxidation experienced by the wild-type protein relative to a kinetically trapped, three-helical folding intermediate and an unfolded variant that lacks secondary structure. Analysis of the unfolded variant by FPOP-MS shows oxidative modifications consistent with the species adopting a solution conformation with a high degree of solvent accessibility. The folding intermediate, by contrast, experiences increased levels of oxidation relative to the wild-type, native protein only in regions destabilised by the amino acid substitutions introduced. The results demonstrate the utility of FPOP-MS to characterise protein variants in different conformational states and to provide insights into protein folding mechanisms that are complementary to measurements such as hydrogen/deuterium exchange labelling and Φ-value analysis.
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