Interaction between Nonhistone Protein HMGB1 and Linker Histone H1 Facilitates the Formation of Structurally Ordered DNA-Protein Complexes

<table>AFM height trace images of DNA-HMGB1/H1 complexes taken in a tapping mode on mica. DNA to protein ratios <svg height="10.325" id="M9" style="vertical-align:-0.0pt" version="1.1" viewbox="0 0 11.6875 10.325" width="11.6875" xmlns="http://www.w3.org/2000/svg">
<g transform="matrix(1.25,0,0,-1.25,0,10.325)">
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<tspan style="font-size: 12.50px; " x="0" y="0">𝑅</tspan>
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</svg>, defined as the number of DNA base pairs per one protein molecule in the complex was 35 : 1. HMGB1 : H1 molar ratio is 1 : 1. The bar scale corresponds to 100 nm.</table>

Journal of Spectroscopy

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Figure 3

Figure 3: Interaction between Nonhistone Protein HMGB1 and Linker Histone H1 Facilitates the Formation of Structurally Ordered DNA-Protein Complexes 