Articles | Volume 3, issue 1
https://doi.org/10.5194/mr-3-101-2022
© Author(s) 2022. 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-3-101-2022
© Author(s) 2022. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
The effect of spin polarization on double electron–electron resonance (DEER) spectroscopy
Sarah R. Sweger
Department of Chemistry, University of Washington, Seattle, WA 98195, USA
Vasyl P. Denysenkov
Institute of Physical and Theoretical Chemistry and Center of Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, Frankfurt, Germany
Lutz Maibaum
Department of Chemistry, University of Washington, Seattle, WA 98195, USA
Thomas F. Prisner
Institute of Physical and Theoretical Chemistry and Center of Biomolecular Magnetic Resonance, Goethe University Frankfurt am Main, Frankfurt, Germany
Department of Chemistry, University of Washington, Seattle, WA 98195, USA
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Vasyl Denysenkov, Alexey Fedotov, Burkhard Endeward, and Thomas F. Prisner
Magn. Reson., 7, 21–28, https://doi.org/10.5194/mr-7-21-2026, https://doi.org/10.5194/mr-7-21-2026, 2026
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The developed probe head, which is a combination of the bimodal resonator operating in transmission mode and the low-noise amplifier, led to at least a 2-fold improvement in the sensitivity of the electron paramagnetic resonance spectrometer independent of sample temperature. The probe head is compatible with commercial Bruker spectrometers without their modification.
Paul A. S. Trenkler, Burkhard Endeward, Snorri T. Sigurdsson, and Thomas F. Prisner
Magn. Reson., 6, 281–315, https://doi.org/10.5194/mr-6-281-2025, https://doi.org/10.5194/mr-6-281-2025, 2025
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Pulsed electron paramagnetic resonance can measure distances and orientation between two paramagnetic markers. If they are rigidly attached to a biomolecule, advanced insights into the structure and dynamics of the biomolecule follow. We used chirp pulses to perform real two-dimensional experiments with much shorter experimental time compared to experiments with monochromatic microwave pulses. We also present new pulse sequences and give a detailed protocol for setting up such experiments.
Deniz Sezer, Danhua Dai, and Thomas F. Prisner
Magn. Reson., 4, 243–269, https://doi.org/10.5194/mr-4-243-2023, https://doi.org/10.5194/mr-4-243-2023, 2023
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We recently liberated the solid effect of dynamic nuclear polarization (DNP) from its perturbative treatment by describing the relevant spin dynamics in a time domain. This allows us to easily account for dynamical processes that modulate the spin interactions in liquids, like the translational diffusion of spins. Here we additionally model the slow rotational diffusion of the polarizing agent and analyze DNP data from nitroxide spin labels in lipid bilayers at 9.4 T.
Thorsten Bahrenberg, Samuel M. Jahn, Akiva Feintuch, Stefan Stoll, and Daniella Goldfarb
Magn. Reson., 2, 161–173, https://doi.org/10.5194/mr-2-161-2021, https://doi.org/10.5194/mr-2-161-2021, 2021
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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).
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Short summary
This work examines the physics underlying double electron–electron resonance (DEER) spectroscopy, a magnetic-resonance method that provides nanoscale data about protein structure and conformations.
This work examines the physics underlying double electron–electron resonance (DEER)...