Articles | Volume 2, issue 1
Research article
21 Apr 2021
Research article |  | 21 Apr 2021

Characterization of nucleosome sediments for protein interaction studies by solid-state NMR spectroscopy

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

Related subject area

Field: Solid-state NMR | Topic: Applications – biological macromolecules
Relaxation-induced dipolar exchange with recoupling (RIDER) distortions in CODEX experiments
Alexey Krushelnitsky and Kay Saalwächter
Magn. Reson., 1, 247–259,,, 2020
Short summary

Cited articles

Ader, C., Frey, S., Maas, W., Schmidt, H. B., Gorlich, D., and Baldus, M.: Amyloid-like interactions within nucleoporin FG hydrogels, P. Natl. Acad. Sci. USA, 107, 6281–6285,, 2010. 
Adhireksan, Z., Sharma, D., Lee, P. L., and Davey, C. A.: Near-atomic resolution structures of interdigitated nucleosome fibres, Nat. Commun., 11, 4747,, 2020. 
Allahverdi, A., Yang, R., Korolev, N., Fan, Y., Davey, C. A., Liu, C.-F. F., and Nordenskiöld, L.: The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association, Nucleic Acids Res., 39, 1680–1691,, 2011. 
Allahverdi, A., Chen, Q., Korolev, N., and Nordenskiöld, L.: Chromatin compaction under mixed salt conditions: Opposite effects of sodium and potassium ions on nucleosome array folding, Sci. Rep., 5, 8512,, 2015. 
Allen, H. F., Wade, P. A., and Kutateladze, T. G.: The NuRD architecture, Cell. Mol. Life Sci., 70, 3513–3524,, 2013. 
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.