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

Biophysics and medical physics

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.