ArticleApplied magnetic resonance2010
Resolving Conformational and Rotameric Exchange in Spin-Labeled Proteins Using Saturation Recovery EPR.
Article in Applied magnetic resonance, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Hidden protein disorder: Deciphering the structural organisation and dynamics of a non-canonical CP12 from the diatom Thalassiosira pseudonana.The FEBS journal · 2025Article
- Tracking Copper sensing operon Repressor (CsoR) oligomerization in solution using Electron Paramagnetic Resonance spectroscopy.Protein science : a publication of the Protein Society · 2025Article
- 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
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.Protein science : a publication of the Protein Society · 2024Article
- Review
- A pressure-jump EPR system to monitor millisecond conformational exchange rates of spin-labeled proteins.bioRxiv : the preprint server for biology · 2024Article
- A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins.Applied magnetic resonance · 2024Article
- Guidelines for the Simulations of Nitroxide X-Band cw EPR Spectra from Site-Directed Spin Labeling Experiments Using SMolecules (Basel, Switzerland) · 2023Article
- Structural and dynamic origins of ESR lineshapes in spin-labeled GB1 domain: the insights from spin dynamics simulations based on long MD trajectories.Scientific reports · 2020Article
- An x-band continuous wave saturation recovery electron paramagnetic resonance spectrometer based on an arbitrary waveform generator.The Review of scientific instruments · 2019Article
- Effect of Phosphorylation on Interactions between Transmembrane Domains of SERCA and Phospholamban.Biophysical journal · 2018Article
- A Budding-Defective M2 Mutant Exhibits Reduced Membrane Interaction, Insensitivity to Cholesterol, and Perturbed Interdomain Coupling.Biochemistry · 2017Article
- Cholesterol-Dependent Conformational Exchange of the C-Terminal Domain of the Influenza A M2 Protein.Biochemistry · 2015Article
- Structure-relaxation mechanism for the response of T4 lysozyme cavity mutants to hydrostatic pressure.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Visualizing transient dark states by NMR spectroscopy.Quarterly reviews of biophysics · 2015Article
- Stationary-phase EPR for exploring protein structure, conformation, and dynamics in spin-labeled proteins.Biochemistry · 2014Article
- Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy.Journal of the American Chemical Society · 2014Article
- Identifying and quantitating conformational exchange in membrane proteins using site-directed spin labeling.Accounts of chemical research · 2014Review
- Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The function of many proteins involves equilibria between conformational substates, and to elucidate mechanisms of function it is essential to have experimental tools to detect the presence of conformational substates and to determine the time scale of exchange between them. Site-directed spin labeling (SDSL) has the potential to serve this purpose. In proteins containing a nitroxide side chain (R1), multicomponent electron paramagnetic resonance (EPR) spectra can arise either from equilibria involving different conformational substates or rotamers of R1. To employ SDSL to uniquely identify conformational equilibria, it is thus essential to distinguish between these origins of multicomponent spectra. Here we show that this is possible based on the time scale for exchange of the nitroxide between distinct environments that give rise to multicomponent EPR spectra; rotamer exchange for R1 lies in the ≈0.1-1 μs range, while conformational exchange is at least an order of magnitude slower. The time scales of exchange events are determined by saturation recovery EPR, and in favorable cases, the exchange rate constants between substates with lifetimes of approximately 1-70 μs can be estimated by the approach.
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Registered trials
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