Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-161-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
https://doi.org/10.5194/mr-2-161-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
The decay of the refocused Hahn echo in double electron–electron resonance (DEER) experiments
Thorsten Bahrenberg
Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot 7610001, Israel
Samuel M. Jahn
Department of Chemistry, University of Washington, Seattle, Washington 98195, USA
Akiva Feintuch
Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot 7610001, Israel
Department of Chemistry, University of Washington, Seattle, Washington 98195, USA
Daniella Goldfarb
CORRESPONDING AUTHOR
Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot 7610001, Israel
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Cited
14 citations as recorded by crossref.
- Milliwatt three- and four-pulse double electron electron resonance for protein structure determination M. Teucher et al. 10.1039/D1CP05508A
- dHis-troying Barriers: Deuteration Provides a Pathway to Increase Sensitivity and Accessible Distances for Cu2+ Labels J. Casto et al. 10.1021/acs.jpclett.1c01002
- Nuclear pair electron spin echo envelope modulation G. Jeschke 10.1016/j.jmro.2023.100094
- PELDOR to the Metal: Cu(II)-Based Labels Put a New Spin on Distance Measurements J. Casto et al. 10.1007/s00723-024-01658-8
- Inter-pulse delay optimization for dynamical decoupling pulse sequences with up to six refocusing pulses G. Horvat et al. 10.1140/epjp/s13360-021-01832-y
- Regularized dynamical decoupling noise spectroscopy – a decoherence descriptor for radicals in glassy matrices J. Soetbeer et al. 10.1039/D1CP03103A
- Exploring tunneling ESEEM beyond methyl groups in nitroxides at low temperatures A. Eggeling et al. 10.1039/D4CP01212G
- A systematic study on the effect of protonation and deuteration on electron spin Tm/T2 in a cellular context F. Torricella et al. 10.1039/D4CP00599F
- Evolution of CPEB4 Dynamics Across its Liquid–Liquid Phase Separation Transition M. Seal et al. 10.1021/acs.jpcb.1c06696
- Temperature-Dependent Rotation of Protonated Methyl Groups in Otherwise Deuterated Proteins Modulates DEER Distance Distributions T. Schmidt & V. Stadnytskyi 10.1007/s00723-024-01720-5
- Gadolinium Spin Decoherence Mechanisms at High Magnetic Fields C. Wilson et al. 10.1021/acs.jpclett.3c01847
- Intermolecular contributions, filtration effects and signal composition of SIFTER (single-frequency technique for refocusing) A. Vanas et al. 10.5194/mr-4-1-2023
- Mechanism of Electron Spin Decoherence in a Partially Deuterated Glassy Matrix S. Jahn et al. 10.1021/acs.jpclett.2c00939
- The contribution of methyl groups to electron spin decoherence of nitroxides in glassy matrices S. Jahn et al. 10.1063/5.0240801
14 citations as recorded by crossref.
- Milliwatt three- and four-pulse double electron electron resonance for protein structure determination M. Teucher et al. 10.1039/D1CP05508A
- dHis-troying Barriers: Deuteration Provides a Pathway to Increase Sensitivity and Accessible Distances for Cu2+ Labels J. Casto et al. 10.1021/acs.jpclett.1c01002
- Nuclear pair electron spin echo envelope modulation G. Jeschke 10.1016/j.jmro.2023.100094
- PELDOR to the Metal: Cu(II)-Based Labels Put a New Spin on Distance Measurements J. Casto et al. 10.1007/s00723-024-01658-8
- Inter-pulse delay optimization for dynamical decoupling pulse sequences with up to six refocusing pulses G. Horvat et al. 10.1140/epjp/s13360-021-01832-y
- Regularized dynamical decoupling noise spectroscopy – a decoherence descriptor for radicals in glassy matrices J. Soetbeer et al. 10.1039/D1CP03103A
- Exploring tunneling ESEEM beyond methyl groups in nitroxides at low temperatures A. Eggeling et al. 10.1039/D4CP01212G
- A systematic study on the effect of protonation and deuteration on electron spin Tm/T2 in a cellular context F. Torricella et al. 10.1039/D4CP00599F
- Evolution of CPEB4 Dynamics Across its Liquid–Liquid Phase Separation Transition M. Seal et al. 10.1021/acs.jpcb.1c06696
- Temperature-Dependent Rotation of Protonated Methyl Groups in Otherwise Deuterated Proteins Modulates DEER Distance Distributions T. Schmidt & V. Stadnytskyi 10.1007/s00723-024-01720-5
- Gadolinium Spin Decoherence Mechanisms at High Magnetic Fields C. Wilson et al. 10.1021/acs.jpclett.3c01847
- Intermolecular contributions, filtration effects and signal composition of SIFTER (single-frequency technique for refocusing) A. Vanas et al. 10.5194/mr-4-1-2023
- Mechanism of Electron Spin Decoherence in a Partially Deuterated Glassy Matrix S. Jahn et al. 10.1021/acs.jpclett.2c00939
- The contribution of methyl groups to electron spin decoherence of nitroxides in glassy matrices S. Jahn et al. 10.1063/5.0240801
Latest update: 23 Nov 2024
Short summary
Double electron–electron resonance (DEER) provides information on the structure of proteins by attaching two spin labels to the protein at a well-defined location and measuring the distance between them. The sensitivity of the method in terms of the amount of the protein that is needed for the experiment depends strongly on the relaxation properties of the spin label and the composition of the solvent. We show how to set up the experiment for best sensitivity when the solvent is water (H2O).
Double electron–electron resonance (DEER) provides information on the structure of proteins by...