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

<table>CD spectra of DNA and its complexes with non-histone protein HMGB1 and histone H1 at different DNA to protein ratios <svg height="10.325" id="M6" 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">
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</svg>, defined as the number of DNA base pairs per one protein molecule in the complex. The complexes with the ratios 175 : 1; 140 : 1; 70 : 1; 10 : 1 are marked in the plot. Concentration of DNA in all samples was 0.06 mg/mL; the optical path length was 0.5 cm. The molar ratio of HMGB1 to H1 in the samples was maintained 1 : 1.</table>

Journal of Spectroscopy

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Figure 1

Figure 1: Interaction between Nonhistone Protein HMGB1 and Linker Histone H1 Facilitates the Formation of Structurally Ordered DNA-Protein Complexes 