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. 2019 Jun 17;24(12):2258. doi: 10.3390/molecules24122258

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Interaction of AtNRP1/AtNRP2 with histone H2A-H2B dimer. Electrophoretic mobility shift assay for the binding of histone dimer with (a) full-length AtNRP1 and (b) full-length AtNRP2. (c) The binding isotherm of full-length AtNRP1: H2A-H2B. (d) The binding isotherm of full-length AtNRP2: H2A-H2B. The top panel represents the sequential injection of AtH2A-H2B into AtNRP1 and bottom represents integrated heat data after correction for the heat of dilution. The data fitting was done using sequential binding model. (Red rectangles represent experimental fit and grey circles represent actual fit).