ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2014
The spatial effect of protein deuteration on nitroxide spin-label relaxation: implications for EPR distance measurement.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- SOQS: Superposition of Quantum States for Selective Detection of Dipolar Frequency Multiples in Pulsed EPR Spectroscopy.ACS physical chemistry Au · 2026Article
- Direct observation and measurement of the average quantum methyl-tunneling frequency in a protein usingChemical communications (Cambridge, England) · 2026Article
- Quantifying the liquid-liquid transition in cold water/glycerol mixtures by intermolecular hyperfine relaxation-induced dipolar modulation enhancement (ih-RIDME).Physical chemistry chemical physics : PCCP · 2025Article
- A fluorescent-protein spin qubit.Nature · 2025Article
- Q-Band Double Quantum Coherence ESR for Sensitive Nitroxide-Based Distance Measurements.The journal of physical chemistry. B · 2025Article
- Flavoproteins as native and genetically encoded spin probes for in cell ESR spectroscopy.Nature communications · 2025Article
- Molecular Design for Optically Induced Magnetization: Targeting Excited State Orbital Degeneracy in Tungsten(V) Complexes.Journal of the American Chemical Society · 2025Article
- Temperature-Dependent Rotation of Protonated Methyl Groups in Otherwise Deuterated Proteins Modulates DEER Distance Distributions.Applied magnetic resonance · 2025Article
- Quantifying methyl tunneling induced (de)coherence of nitroxides in glassyPhysical chemistry chemical physics : PCCP · 2023Article
- Quantitative analysis of sterol-modulated monomer-dimer equilibrium of the βProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to CaProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Long-range distance determination in fully deuterated RNA with pulsed EPR spectroscopy.Biophysical journal · 2022Article
- Benchmark Test and Guidelines for DEER/PELDOR Experiments on Nitroxide-Labeled Biomolecules.Journal of the American Chemical Society · 2021Article
- A Chiral Lanthanide Tag for Stable and Rigid Attachment to Single Cysteine Residues in Proteins for NMR, EPR and Time-Resolved Luminescence Studies.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- The decay of the refocused Hahn echo in double electron-electron resonance (DEER) experiments.Magnetic resonance (Gottingen, Germany) · 2021Article
- Do the P1 and P2 hairpins of the Guanidine-II riboswitch interact?Nucleic acids research · 2020Article
- Article
- Electron Spin Relaxation of Photoexcited Porphyrin in Water-Glycerol Glass.Molecules (Basel, Switzerland) · 2020Article
- Site-Directed Spin Labeling of RNA with aMolecules (Basel, Switzerland) · 2019Article
- Fast electron paramagnetic resonance magic angle spinning simulations using analytical powder averaging techniques.The Journal of chemical physics · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Pulsed electron-electron double resonance (PELDOR) coupled with site-directed spin labeling is a powerful technique for the elucidation of protein or nucleic acid, macromolecular structure and interactions. The intrinsic high sensitivity of electron paramagnetic resonance enables measurement on small quantities of bio-macromolecules, however short relaxation times impose a limit on the sensitivity and size of distances that can be measured using this technique. The persistence of the electron spin-echo, in the PELDOR experiment, is one of the most crucial limitations to distance measurement. At a temperature of around 50 K one of the predominant factors affecting persistence of an echo, and as such, the sensitivity and measurable distance between spin labels, is the electron spin echo dephasing time (Tm). It has become normal practice to use deuterated solvents to extend Tm and recently it has been demonstrated that deuteration of the underlying protein significantly extends Tm. Here we examine the spatial effect of segmental deuteration of the underlying protein, and also explore the concentration and temperature dependence of highly deuterated systems.
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