Articles | Volume 5, issue 1
https://doi.org/10.5194/mr-5-69-2024
© Author(s) 2024. 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-5-69-2024
© Author(s) 2024. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
Research article
| 
11 Jun 2024
Research article |
| 11 Jun 2024
| 11 Jun 2024
Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR
Kathrin Aebischer
Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland
Lea Marie Becker
Institute of Science and Technology Austria (ISTA), Am Campus 1, 3400 Klosterneuburg, Austria
Paul Schanda
Institute of Science and Technology Austria (ISTA), Am Campus 1, 3400 Klosterneuburg, Austria
Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 2, 8093 Zurich, Switzerland
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The radio-frequency (rf) field amplitude in solid-state NMR probes changes over the sample volume, i.e. different parts of the sample will experience different nutation frequencies. If the sample is rotated inside the coil as it is typical for magic angle spinning in solid-state NMR, such a position-dependent inhomogeneity leads to an additional time dependence of the rf field amplitude. We show that such time-dependent modulations do not play an important role in many experiments.
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Resonant pulses in a spin-lock frame are used to select parts of the rf-field distribution in NMR experiments. Such pulses can be implemented in a straightforward way and arbitrarily shaped pulses can be used. We show an application of such pulses in homonuclear decoupling where restricting the amplitude distribution of the rf field leads to improved performance.
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Protons (1H) are useful reporters of protein structure and dynamics in solid-state NMR. However, 1H abundance is detrimental to the resolution of NMR spectra. Substituting 1H by deuterons has been an efficient strategy to improve spectral quality, but when the crucial backbone amide sites are not protonated, much information is loss. We propose a method to completely protonate the amide sites, while maintaining high-resolution information, which partially also extends to backbone alpha-1H.
Aaron Himmler, Mohammed M. Albannay, Gevin von Witte, Sebastian Kozerke, and Matthias Ernst
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Dynamic nuclear polarization requires a waveguide that connects the cold (1–10 K) sample space to the outside. To reduce the heating of the sample, a waveguide is produced from steel which has low thermal conductivity but attenuates the microwaves. Therefore, the inside of the waveguide should be plated with silver to reduce electrical losses. We show a new simple way to electroplate such waveguides with a thin silver layer and show that this improves the experimental performance.
Václav Římal, Morgane Callon, Alexander A. Malär, Riccardo Cadalbert, Anahit Torosyan, Thomas Wiegand, Matthias Ernst, Anja Böckmann, and Beat H. Meier
Magn. Reson., 3, 15–26, https://doi.org/10.5194/mr-3-15-2022, https://doi.org/10.5194/mr-3-15-2022, 2022
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Through the advent of fast magic-angle spinning and high magnetic fields, the spectral resolution of solid-state NMR spectra has recently been greatly improved. To take full advantage of this gain, the magnetic field must be stable over the experiment time of hours or even days. We thus monitor the field by simultaneous acquisition of a frequency reference (SAFR) and use this information to correct multidimensional spectra improving resolution and availability of productive magnet time.
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Magn. Reson., 2, 523–543, https://doi.org/10.5194/mr-2-523-2021, https://doi.org/10.5194/mr-2-523-2021, 2021
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The radio-frequency (rf) field amplitude in solid-state NMR probes changes over the sample volume, i.e. different parts of the sample will experience different nutation frequencies. If the sample is rotated inside the coil as it is typical for magic angle spinning in solid-state NMR, such a position-dependent inhomogeneity leads to an additional time dependence of the rf field amplitude. We show that such time-dependent modulations do not play an important role in many experiments.
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Sample rotation around the magic angle averages out the dipolar couplings in homonuclear spin systems in a first-order approximation. However, in higher orders, residual coupling terms remain and lead to a broadening of the spectral lines. We investigate the source of this broadening and the effects on the powder line shape in small spin systems with and without chemical shifts. We show that one can expect different scaling behavior as a function of the spinning frequency for the two cases.
Alicia Vallet, Adrien Favier, Bernhard Brutscher, and Paul Schanda
Magn. Reson., 1, 331–345, https://doi.org/10.5194/mr-1-331-2020, https://doi.org/10.5194/mr-1-331-2020, 2020
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We introduce ssNMRlib, a library of pulse sequences and jython scripts for user-friendly setup and acquisition of solids-state NMR experiments. ssNMRlib facilitates all steps of data acquisition, including calibration of various pulse-sequence parameters and semi-automatic setup of even complex high-dimensional experiments, using an intuitive graphical user interface, launched directly within Bruker's Topspin acquisition program.
Kathrin Aebischer, Nino Wili, Zdeněk Tošner, and Matthias Ernst
Magn. Reson., 1, 187–195, https://doi.org/10.5194/mr-1-187-2020, https://doi.org/10.5194/mr-1-187-2020, 2020
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Resonant pulses in a spin-lock frame are used to select parts of the rf-field distribution in NMR experiments. Such pulses can be implemented in a straightforward way and arbitrarily shaped pulses can be used. We show an application of such pulses in homonuclear decoupling where restricting the amplitude distribution of the rf field leads to improved performance.
Johannes Hellwagner, Liam Grunwald, Manuel Ochsner, Daniel Zindel, Beat H. Meier, and Matthias Ernst
Magn. Reson., 1, 13–25, https://doi.org/10.5194/mr-1-13-2020, https://doi.org/10.5194/mr-1-13-2020, 2020
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This paper analyzes a commonly used line-narrowing mechanism (homonuclear decoupling) in solid-state NMR and discusses what limits the achievable line width. Based on theoretical considerations, the contribution of different effects to the line width is discussed and a new contributing term is identified. This research allows us to evaluate new ways to improve the line width in such homonuclear decoupled spectra.
Related subject area
Field: Solid-state NMR | Topic: Applications – biological macromolecules
Characterization of nucleosome sediments for protein interaction studies by solid-state NMR spectroscopy
Relaxation-induced dipolar exchange with recoupling (RIDER) distortions in CODEX experiments
Ulric B. le Paige, ShengQi Xiang, Marco M. R. M. Hendrix, Yi Zhang, Gert E. Folkers, Markus Weingarth, Alexandre M. J. J. Bonvin, Tatiana G. Kutateladze, Ilja K. Voets, Marc Baldus, and Hugo van Ingen
Magn. Reson., 2, 187–202, https://doi.org/10.5194/mr-2-187-2021, https://doi.org/10.5194/mr-2-187-2021, 2021
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NMR studies can be of great help in understanding the molecular mechanisms of nucleosome functions. For solid-state NMR, nucleosomes need to be tightly packed together. We show that centrifugation of nucleosomes results in formation of gels with very high packing ratios yet without pronounced order in the packing and without formation of specific or stable inter-nucleosome contacts. This makes the approach suitable also for the study of proteins that bind weakly to the nucleosome.
Alexey Krushelnitsky and Kay Saalwächter
Magn. Reson., 1, 247–259, https://doi.org/10.5194/mr-1-247-2020, https://doi.org/10.5194/mr-1-247-2020, 2020
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This work presents systematic methodological study of one of the types of the nuclear magnetic resonance experiments that enables study of molecular dynamics on a millisecond timescale. A modification of a standard experiment was suggested that excludes possible artefacts and distortions. It has been demonstrated that the standard experiment reveals slow overall motion of proteins in a rigid crystal lattice, whereas the artefact-free experimental setup demonstrates that the proteins are rigid.
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Short summary
To characterize the amplitude of dynamic processes in molecules, anisotropic parameters can be measured using solid-state NMR. However, the timescales of motion that lead to such a scaling of the anisotropic interactions are not clear. Using numerical simulations in small spin systems, we could show that mostly the magnitude of the anisotropic interaction determines the range of timescales detected by the scaled anisotropic interaction, and experimental parameters play a very minor role.
To characterize the amplitude of dynamic processes in molecules, anisotropic parameters can be...
