ArticleBiophysical journal2005
Accessibility and dynamics of nitroxide side chains in T4 lysozyme measured by saturation recovery EPR.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- EPR Techniques to Probe Insertion and Conformation of Spin-Labeled Proteins in Lipid Bilayers.Methods in molecular biology (Clifton, N.J.) · 2026Article
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- Core-shell model of the clusters of CPEB4 isoforms preceding liquid-liquid phase separation.Biophysical journal · 2024Article
- Site-directed spin label EPR studies of the structure and membrane interactions of the bacterial phospholipase ExoU.Applied magnetic resonance · 2024Article
- Spin-labeling Insights into How Chemical Fixation Impacts Glycan Organization on Cells.Applied magnetic resonance · 2024Article
- Conformational Differences Are Observed for the Active and Inactive Forms of Pinholin SThe journal of physical chemistry. B · 2020Article
- Structural Dynamics and Topology of the Inactive Form of SThe journal of physical chemistry. B · 2020Article
- Continuous Wave Electron Paramagnetic Resonance Spectroscopy Reveals the Structural Topology and Dynamic Properties of Active Pinholin SThe journal of physical chemistry. B · 2019Article
- Conformational Changes and Membrane Interaction of the Bacterial Phospholipase, ExoU: Characterization by Site-Directed Spin Labeling.Cell biochemistry and biophysics · 2019Article
- Effect of Phosphorylation on Interactions between Transmembrane Domains of SERCA and Phospholamban.Biophysical journal · 2018Article
- Optimal Tikhonov regularization for DEER spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2018Article
- Cholesterol-Dependent Conformational Exchange of the C-Terminal Domain of the Influenza A M2 Protein.Biochemistry · 2015Article
- Peptide-Membrane Interactions by Spin-Labeling EPR.Methods in enzymology · 2015Article
- Stationary-phase EPR for exploring protein structure, conformation, and dynamics in spin-labeled proteins.Biochemistry · 2014Article
- Electron paramagnetic resonance spectroscopy of nitroxide-labeled calmodulin.The protein journal · 2014Article
- Conformational selection and adaptation to ligand binding in T4 lysozyme cavity mutants.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Probing Protein Secondary Structure using EPR: Investigating a Dynamic Region of Visual Arrestin.Applied magnetic resonance · 2012Article
- Resolving Conformational and Rotameric Exchange in Spin-Labeled Proteins Using Saturation Recovery EPR.Applied magnetic resonance · 2010Article
- Paramagnetic relaxation enhancements in unfolded proteins: theory and application to drkN SH3 domain.Protein science : a publication of the Protein Society · 2009Article
- A paramagnetic molecular voltmeter.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
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5 authors.
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Abstract
Long pulse saturation recovery electron paramagnetic resonance spectroscopy is applied to the investigation of spin-labeled side chains placed along a regular helix extending from 128 to 135 in T4 lysozyme. Under an argon atmosphere, analysis of the exponential saturation recovery curves gives the spin-lattice relaxation rates of the nitroxides, which depend on the nitroxide side-chain dynamics. In the presence of the fast-relaxing paramagnetic reagents O(2) or NiEDDA, global analysis of the saturation recovery provides the spin-lattice relaxation rates as well as the Heisenberg exchange rates of the nitroxide with the reagents. As previously shown with power saturation methods, such exchange rates are direct measures of the solvent accessibility of the nitroxide side chains in the protein structure. The periodic dependence of the spin-lattice relaxation rates and the exchange rates along the 128-135 sequence reveal the presence of the helical structure, demonstrating the use of these parameters in structure determination. In general, multiple exponentials are required to fit the saturation recovery data, thus identifying multiple states of the side chain. In one case, multiple conformations detected in the spectrum are not evident in the saturation recovery, suggesting rapid exchange on the timescale of spin-lattice relaxation.
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