ArticleMolecular & cellular proteomics : MCP2009
Elucidating in vivo structural dynamics in integral membrane protein by hydroxyl radical footprinting.
Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed.
- Rational tuning of temperature sensitivity of the TRPM8 channel.EMBO reports · 2025Article
- Quantitative readout of methionine residue solvent accessibility in E. coli cells using radiolytic hydroxyl radical labeling and mass spectrometry.Biochemical and biophysical research communications · 2025Article
- In-Cell Fast Photochemical Oxidation Interrogates the Native Structure of Integral Membrane Proteins.Angewandte Chemie (International ed. in English) · 2025Article
- Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions.Analytical methods : advancing methods and applications · 2025Article
- Systematic Fe(II)-EDTA Method of Dose-Dependent Hydroxyl Radical Generation for Protein Oxidative Footprinting.Analytical chemistry · 2023Article
- Precursor Reagent Hydrophobicity Affects Membrane Protein Footprinting.Journal of the American Society for Mass Spectrometry · 2023Article
- An automated liquid jet for fluorescence dosimetry and microsecond radiolytic labeling of proteins.Communications biology · 2022Article
- Characterizing Endogenous Protein Complexes with Biological Mass Spectrometry.Chemical reviews · 2022Review
- Review
- Review
- MEMBRANE PROTEIN STRUCTURES AND INTERACTIONS FROM COVALENT LABELING COUPLED WITH MASS SPECTROMETRY.Mass spectrometry reviews · 2022Review
- Fenton-Chemistry-Based Oxidative Modification of Proteins Reflects Their Conformation.International journal of molecular sciences · 2021Article
- Determination of the glycoprotein specificity of lectins on cell membranes through oxidative proteomics.Chemical science · 2020Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Computational methods in mass spectrometry-based structural proteomics for studying protein structure, dynamics, and interactions.Computational and structural biotechnology journal · 2020Review
- Membrane Protein Structure in Live Cells: Methodology for Studying Drug Interaction by Mass Spectrometry-Based Footprinting.Biochemistry · 2018Article
- Fast Photochemical Oxidation of Proteins Maps the Topology of Intrinsic Membrane Proteins: Light-Harvesting Complex 2 in a Nanodisc.Analytical chemistry · 2016Article
- Mass spectrometry for the biophysical characterization of therapeutic monoclonal antibodies.FEBS letters · 2014Review
- Fast photochemical oxidation of proteins for comparing solvent-accessibility changes accompanying protein folding: data processing and application to barstar.Biochimica et biophysica acta · 2013Article
- Reproducible method to enrich membrane proteins with high purity and high yield for an LC-MS/MS approach in quantitative membrane proteomics.Electrophoresis · 2013Article
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Authors and funding
9 authors.
Funding
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Abstract
We describe here a novel footprinting technique to probe the in vivo structural dynamics of membrane protein. This method utilized in situ generation of hydroxyl radicals to oxidize and covalently modify biomolecules on living Escherichia coli cell surface. After enriching and purifying the membrane proteome, the modified amino acid residues of the protein were identified with tandem mass spectrometry to map the solvent-accessible surface of the protein that will form the footprint of in vivo structure of the protein. Of about 100 outer membrane proteins identified, we investigated the structure details of a typical beta-barrel structure, the porin OmpF. We found that six modified tryptic peptides of OmpF were reproducibly detected with 19 amino acids modified under the physiological condition. The modified amino acid residues were widely distributed in the external loop area, beta-strands, and periplasmic turning area, and all of them were validated as solvent-accessible according to the crystallography data. We further extended this method to study the dynamics of the voltage gating of OmpF in vivo using mimic changes of physiological circumstance either by pH or by ionic strength. Our data showed the voltage gating of porin OmpF in vivo for the first time and supported the proposed mechanism that the local electrostatic field changes in the eyelet region may alter the porin channels to switch. Thus, this novel method can be a potentially efficient method to study the structural dynamics of the membrane proteins of a living cell.
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