Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-187-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
Special issue:
https://doi.org/10.5194/mr-2-187-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
Research article
| 
21 Apr 2021
Research article |
| 21 Apr 2021
| 21 Apr 2021
Characterization of nucleosome sediments for protein interaction studies by solid-state NMR spectroscopy
Ulric B. le Paige
Utrecht NMR Group, Bijvoet Centre for Biomolecular Research,
Utrecht University, 3584 CH, Utrecht, the Netherlands
ShengQi Xiang
Utrecht NMR Group, Bijvoet Centre for Biomolecular Research,
Utrecht University, 3584 CH, Utrecht, the Netherlands
current address: MOE Key Lab for Membrane-less Organelles &
Cellular Dynamics, School of Life Sciences, University of Science and
Technology of China, 96 Jinzhai Road, Hefei, 230026, Anhui, China
Marco M. R. M. Hendrix
Laboratory of Self-Organizing Soft Matter, Department of Chemical
Engineering and Chemistry & Institute for Complex Molecular Systems,
Eindhoven University of Technology, P.O. Box 513, 5600 MB, Eindhoven, the
Netherlands
Yi Zhang
Department of Pharmacology, University of Colorado School of
Medicine, Aurora, CO 80045, USA
Gert E. Folkers
Utrecht NMR Group, Bijvoet Centre for Biomolecular Research,
Utrecht University, 3584 CH, Utrecht, the Netherlands
Markus Weingarth
Utrecht NMR Group, Bijvoet Centre for Biomolecular Research,
Utrecht University, 3584 CH, Utrecht, the Netherlands
Alexandre M. J. J. Bonvin
Utrecht NMR Group, Bijvoet Centre for Biomolecular Research,
Utrecht University, 3584 CH, Utrecht, the Netherlands
Tatiana G. Kutateladze
Department of Pharmacology, University of Colorado School of
Medicine, Aurora, CO 80045, USA
Ilja K. Voets
Laboratory of Self-Organizing Soft Matter, Department of Chemical
Engineering and Chemistry & Institute for Complex Molecular Systems,
Eindhoven University of Technology, P.O. Box 513, 5600 MB, Eindhoven, the
Netherlands
Marc Baldus
Utrecht NMR Group, Bijvoet Centre for Biomolecular Research,
Utrecht University, 3584 CH, Utrecht, the Netherlands
Hugo van Ingen
CORRESPONDING AUTHOR
Utrecht NMR Group, Bijvoet Centre for Biomolecular Research,
Utrecht University, 3584 CH, Utrecht, the Netherlands
Related subject area
Field: Solid-state NMR | Topic: Applications – biological macromolecules
Evaluating the motional timescales contributing to averaged anisotropic interactions in MAS solid-state NMR
Relaxation-induced dipolar exchange with recoupling (RIDER) distortions in CODEX experiments
Kathrin Aebischer, Lea Marie Becker, Paul Schanda, and Matthias Ernst
Magn. Reson., 5, 69–86, https://doi.org/10.5194/mr-5-69-2024, https://doi.org/10.5194/mr-5-69-2024, 2024
Short summary
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.
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
Short summary
Short summary
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
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.
NMR studies can be of great help in understanding the molecular mechanisms of nucleosome...
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