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. 2013 Oct 8;42(2):1311–1325. doi: 10.1093/nar/gkt899

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© The Author(s) 2013. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Mass spectrometry analysis of the tryptic peptides obtained from eNP/H3-H4 complexes. (A) 12.5% Tris-Tricine gel electrophoresis of the tryptic peptides obtained from eNP/H3-H4 complexes (1/2 molar ratio). The peptides from the bands highlighted within the box were analyzed by MS/MS. 1, eNP control; 2, eNP digested in 0.24 M NaCl; 3, H3-H4 digested in 2 M NaCl; 4, H3-H4 trypsinized in 0.24 M NaCl; 5, H3-H4 control; 6, eNP/H3-H4 1/2 complex digested in 0.24 M NaCl. All samples were incubated with trypsin during 30 min. (B) Structure of the H3-H4 tetramer as found in the octamer (entry 1TZY in PDB). Shown in white are the tryptic peptides identified by mass spectrometry from H3 (blue) and H4 (red). (C) Amino acid sequence of H3 (accession number 0806228A) and H4 (accession number U37576.1) showing the HFD (gray boxes) and its three helixes (underlined). The peptides protected in the complex (white in panel B) are highlighted in red.