NMR assignments of human linker histone H1x N-terminal domain and globular domain in the presence and absence of perchlorate
Author:
Funder
National Research Foundation
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
http://link.springer.com/content/pdf/10.1007/s12104-019-09886-x.pdf
Reference30 articles.
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2. Bannister AJ, Kouzarides T (2011) Regulation of chromatin by histone modifications. Cell Res 21:381–395. https://doi.org/10.1038/cr.2011.22
3. Bates DL, Thomas JO (1981) Histones H1 and H5: one or two molecules per nucleosome? Nucleic Acids Res 9:5883–5894
4. Böhm L, Mitchell TC (1985) Sequence conservation in the N-terminal domain of histone H1. FEBS Lett 193:1–4
5. Cavanagh J, Fairbrother WJ, Palmer AG, Rance M, Skelton NJ (2007) CHAPTER 7—Heteronuclear NMR experiments, in: Cavanagh J, Fairbrother WJ, Palmer AG, Rance M, Skelton NJ (Eds.), Protein NMR spectroscopy (2 edn). Academic Press, Burlington, pp 533–678. https://doi.org/10.1016/B978-012164491-8/50009-9
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1. Raw nuclear magnetic resonance data of human linker histone H1x, lacking the C-terminal domain (NGH1x), and trajectory data of nanosecond molecular dynamics simulations of GH1x- and NGH1x-chromatosomes;Data in Brief;2020-08
2. Docking data of selected human linker histone variants to the nucleosome;Data in Brief;2020-06
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