ArticleAnalytical chemistry2016
Fast Photochemical Oxidation of Proteins Maps the Topology of Intrinsic Membrane Proteins: Light-Harvesting Complex 2 in a Nanodisc.
Article in Analytical chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Assessment of Protein Conformation via Diazirine-Promoted Oxidation of Methionine and Tryptophan Residues.Analytical chemistry · 2026Article
- In-Cell Fast Photochemical Oxidation Interrogates the Native Structure of Integral Membrane Proteins.Angewandte Chemie (International ed. in English) · 2025Article
- Mass Spectrometry-Based Protein Footprinting for Protein Structure Characterization.Accounts of chemical research · 2025Article
- Quantifying the Impact of the Peptide Identification Framework on the Results of Fast Photochemical Oxidation of Protein Analysis.Journal of proteome research · 2024Article
- 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
- Advances in Mass Spectrometry on Membrane Proteins.Membranes · 2023Review
- Investigating Daptomycin-Membrane Interactions Using Native MS and Fast Photochemical Oxidation of Peptides in Nanodiscs.Analytical chemistry · 2023Article
- Development of Spheroid-FPOP: An In-Cell Protein Footprinting Method for 3D Tumor Spheroids.Journal of the American Society for Mass Spectrometry · 2023Article
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Advances in the Understanding of the Lifecycle of Photosystem II.Microorganisms · 2022Review
- Review
- Investigating Antimicrobial Peptide-Membrane Interactions Using Fast Photochemical Oxidation of Peptides in Nanodiscs.Journal of the American Society for Mass Spectrometry · 2022Article
- MEMBRANE PROTEIN STRUCTURES AND INTERACTIONS FROM COVALENT LABELING COUPLED WITH MASS SPECTROMETRY.Mass spectrometry reviews · 2022Review
- Article
- Bacteriophage-encoded lethal membrane disruptors: Advances in understanding and potential applications.Frontiers in microbiology · 2022Review
- Nanoparticles and photochemistry for native-like transmembrane protein footprinting.Nature communications · 2021Article
- Diethylpyrocarbonate Footprints a Membrane Protein in Micelles.Journal of the American Society for Mass Spectrometry · 2021Article
- Carbocation Footprinting of Soluble and Transmembrane Proteins.Analytical chemistry · 2021Article
- Footprinting Mass Spectrometry of Membrane Proteins: Ferroportin Reconstituted in Saposin A Picodiscs.Analytical chemistry · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Although membrane proteins are crucial participants in photosynthesis and other biological processes, many lack high-resolution structures. Prior to achieving a high-resolution structure, we are investigating whether MS-based footprinting can provide coarse-grained protein structure by following structural changes that occur upon ligand binding, pH change, and membrane binding. Our platform probes topology and conformation of membrane proteins by combining MS-based footprinting, specifically fast photochemical oxidation of proteins (FPOP), and lipid Nanodiscs, which are more similar to the native membrane environment than are the widely used detergent micelles. We describe here results that show a protein's outer membrane regions are more heavily footprinted by OH radicals whereas the regions spanning the lipid bilayer remain inert to the labeling. Nanodiscs generally exhibit more protection of membrane proteins compared to detergent micelles and less shielding to those protein residues that exist outside the membrane. The combination of immobilizing the protein in Nanodiscs and footprinting with FPOP is a feasible approach to map extra-membrane protein surfaces, even at the amino-acid level, and to illuminate intrinsic membrane protein topology.
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