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FIGURE 3. Cooperativity is dependent on both the ionic strength and histone tails. A, Hill plot of H2A/H2B binding yNap1 at ∼0.15 m (closed circles) and ∼0.35 m (open squares-same data in all plots) ionic strength. The slopes of these data result in a nH of 1 ± 0.1 and 2.4 ± 0.2, respectively. B, normalized fluorescence change as a function of histone dimer. Closed circles are tail-less dimers, and open squares are major type histone dimer. Inset of B is the Hill plot of the tail-less (closed circles) and major type (open squares) dimer. The slopes of these data result in an nH of 1.5 ± 0.1 and 1.0 ± 0.1, respectively.

Image published in: Andrews AJ et al. (2008)

Copyright © 2008, The American Society for Biochemistry and Molecular Biology, Inc. This image is reproduced with permission of the journal and the copyright holder. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license

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