ArticleBiophysical journal2009
Pulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Local Organization of Biological Membranes Modulates Tau-Lipid Interactions and Fibril formation.JACS Au · 2026Article
- Crystallographic and EPR-based characterisation of CuInorganic chemistry frontiers · 2026Article
- Electron Paramagnetic Resonance Spectroscopy of Spin-Labeled Lipids for Studying Lipid-Protein Interaction in Model and Biomembranes.Methods in molecular biology (Clifton, N.J.) · 2026Article
- EPR Techniques to Probe Insertion and Conformation of Spin-Labeled Proteins in Lipid Bilayers.Methods in molecular biology (Clifton, N.J.) · 2026Article
- RIDME Spectroscopy: New Topics Beyond the Determination of Electron Spin-Spin Distances.The journal of physical chemistry letters · 2025Review
- ih-RIDME: a pulse EPR experiment to probe the heterogeneous nuclear environment.Magnetic resonance (Gottingen, Germany) · 2025Article
- EPR spectroscopic characterisation of native CuDalton transactions (Cambridge, England : 2003) · 2024Article
- Spectroscopically Orthogonal Labelling to Disentangle Site-Specific Nitroxide Label Distributions.Applied magnetic resonance · 2024Article
- Investigating Native Metal Ion Binding Sites in Mammalian Histidine-Rich Glycoprotein.Journal of the American Chemical Society · 2023Article
- Article
- EPR Spectroscopy Provides New Insights into Complex Biological Reaction Mechanisms.The journal of physical chemistry. B · 2022Review
- HDX-guided EPR spectroscopy to interrogate membrane protein dynamics.STAR protocols · 2022Article
- The Cu(ii) - dietary fibre interactions at molecular level unveiledRSC advances · 2022Article
- Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state.Structure (London, England : 1993) · 2022Article
- A Comparison of Cysteine-Conjugated Nitroxide Spin Labels for Pulse Dipolar EPR Spectroscopy.Molecules (Basel, Switzerland) · 2021Article
- Liquid-Liquid Phase Separation of Tau Driven by Hydrophobic Interaction Facilitates Fibrillization of Tau.Journal of molecular biology · 2021Article
- Investigation of the Hydration State of Self-Assembled Peptide Nanostructures with Advanced Electron Paramagnetic Resonance Spectroscopy.ACS omega · 2019Article
- Tau-Cofactor Complexes as Building Blocks of Tau Fibrils.Frontiers in neuroscience · 2019Article
- Topology of active, membrane-embedded Bax in the context of a toroidal pore.Cell death and differentiation · 2018Article
- MMM: A toolbox for integrative structure modeling.Protein science : a publication of the Protein Society · 2018Article
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5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane proteins reside in a structured environment in which some of their residues are accessible to water, some are in contact with alkyl chains of lipid molecules, and some are buried in the protein. Water accessibility of residues may change during folding or function-related structural dynamics. Several techniques based on the combination of pulsed electron paramagnetic resonance (EPR) with site-directed spin labeling can be used to quantify such water accessibility. Accessibility parameters for different residues in major plant light-harvesting complex IIb are determined by electron spin echo envelope modulation spectroscopy in the presence of deuterated water, deuterium contrast in transversal relaxation rates, analysis of longitudinal relaxation rates, and line shape analysis of electron-spin-echo-detected EPR spectra as well as by the conventional techniques of measuring the maximum hyperfine splitting and progressive saturation in continuous-wave EPR. Systematic comparison of these parameters allows for a more detailed characterization of the environment of the spin-labeled residues. These techniques are applicable independently of protein size and require approximately 10-20 nmol of singly spin-labeled protein per sample. For a residue close to the N-terminus, in a domain unresolved in the existing x-ray structures of light-harvesting complex IIb, all methods indicate high water accessibility.
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