# The changes in the secondary structure of nonhistone HMGB1 protein during the interaction with DNA

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Abstract:

Using circular dichroism spectroscopy and DNA melting analysis we have studied the interaction of non-histone chromosomal protein HMGB1 with high-molecular weight DNA. We have shown, that the degree of the alpha-helicity of the bound HMGB1 is approximately 30 % higher than the alpha-helicity of free HMGB1.