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. 2020 May 1;48(10):5318–5331. doi: 10.1093/nar/gkaa285

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© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — The N-terminal domain within the nucleosome. (A) Illustrations of the most-populated cluster of the NTD from 5-μs BEMD simulations of the full-length hH1.0 within a 211-bp nucleosome. The globular-domain is shown in yellow while the helical-motif within the NTD is in red. The four residues that constitute the basic ‘face’ from the helical-wheel analysis are illustrated. (B) Comparison of the per-residue helicity of the NTD within the nucleosome across different force fields (ff99SB-ildn, ff03ws, Charmm36M (SI Discussion)) and when isolated with neutralized Lys sidechains.