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. 2015 May 20;43(12):5824–5837. doi: 10.1093/nar/gkv507

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© The Author(s) 2015. 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 7. — Removal of histone tails affects binding of TRF1 and TRF2 to TTAGGG repeats adjacent to NCPs. (A, C) Gel mobility-shift assay. Tel2-601-Tel2 NCPs (lanes1–5) and Tel2-601-Tel2 trypsinized NCPs (lanes 6–10) were incubated with increasing amounts of TRF1 (A) and TRF2 (C). The molar concentration of TRF1 and TRF2 is indicated above the lanes. Samples were separated on a 0.8% agarose gel. (B, D) Percentages of unbound NCPs and trypsinized NCPs are reported as a function of protein concentration in the reaction. The concentration of TRF1 (B) and TRF2 (D) at which 50% of naked DNA and nucleosome remain unbound has been extrapolated.