ArticleProceedings of the National Academy of Sciences of the United States of America2011
High-pressure EPR reveals conformational equilibria and volumetric properties of spin-labeled proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 96 citations in OpenAlex.
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- A high-sensitivity stopped-flow EPR system to monitor millisecond conformational kinetics in spin-labeled proteins.Protein science : a publication of the Protein Society · 2025Article
- Capturing protein dynamics across timescales with site-directed spin labeling electron paramagnetic resonance spectroscopy.Current opinion in structural biology · 2025Review
- Effect of Hydrostatic Pressure on theThe journal of physical chemistry letters · 2025Article
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.Protein science : a publication of the Protein Society · 2024Article
- Celebration of 80 years of EPR.Applied magnetic resonance · 2024Article
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.bioRxiv : the preprint server for biology · 2024Article
- Hydration-mediated G-protein-coupled receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- High-Pressure ESR Spectroscopy: On the Rotational Motion of Spin Probes in Pressurized Ionic Liquids.The journal of physical chemistry. B · 2022Article
- Studying KcsA Channel Clustering Using Single Channel Voltage-Clamp Fluorescence Imaging.Frontiers in physiology · 2022Article
- Voronoia 4-ever.Nucleic acids research · 2021Article
- Chemical exchange induced Hahn echo modulation in pulsed electron paramagnetic resonance experiment.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Lessons from pressure denaturation of proteins.Journal of the Royal Society, Interface · 2018Review
- Dynamics of Dystrophin's Actin-Binding Domain.Biophysical journal · 2018Article
- Characterization of and lipopolysaccharide binding to the E. coli LptC protein dimer.Protein science : a publication of the Protein Society · 2018Article
- High-pressure EPR spectroscopy studies of theApplied magnetic resonance · 2017Article
- Powdered G-Protein-Coupled Receptors.The journal of physical chemistry letters · 2016Article
- Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels.Journal of visualized experiments : JoVE · 2016Article
- Conformational Mobility in Cytochrome P450 3A4 Explored by Pressure-Perturbation EPR Spectroscopy.Biophysical journal · 2016Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
Identifying equilibrium conformational exchange and characterizing conformational substates is essential for elucidating mechanisms of function in proteins. Site-directed spin labeling has previously been employed to detect conformational changes triggered by some event, but verifying conformational exchange at equilibrium is more challenging. Conformational exchange (microsecond-millisecond) is slow on the EPR time scale, and this proves to be an advantage in directly revealing the presence of multiple substates as distinguishable components in the EPR spectrum, allowing the direct determination of equilibrium constants and free energy differences. However, rotameric exchange of the spin label side chain can also give rise to multiple components in the EPR spectrum. Using spin-labeled mutants of T4 lysozyme, it is shown that high-pressure EPR can be used to: (i) demonstrate equilibrium between spectrally resolved states, (ii) aid in distinguishing conformational from rotameric exchange as the origin of the resolved states, and (iii) determine the relative partial molar volume (ΔV°) and isothermal compressibility (Δβ(T)) of conformational substates in two-component equilibria from the pressure dependence of the equilibrium constant. These volumetric properties provide insight into the structure of the substates. Finally, the pressure dependence of internal side-chain motion is interpreted in terms of volume fluctuations on the nanosecond time scale, the magnitude of which may reflect local backbone flexibility.
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