Abstract
The conformation of the DNA and histones from calf thymus has been studied both in deoxyribonucleoprotein (DNA · protein) and in the free state using circular dichroism over a wide range of ionic strength, pH and temperature conditions. The relationships between protein content and conformational state of DNA and histones in DNA · protein has been also investigated.The dependence of the circular dichroism on pH and temperature in solutions of DNA, histones and DNA · protein, indicates that DNA and histones in DNA · protein mutually stabilize the secondary structure of each other against denaturation. Changes in the DNA structure within DNA · protein are accompanied by structural transformations of the histones.The circular dichroism study of free DNA and histones in solutions of various ionic strengths shows that the effects produced by DNA on the histone conformation and by histones on the structure of DNA in DNA · protein are similar to that of high ionic strength.The circular dichroism measurements of partial DNA · protein of various protein content show that the structural changes of DNA in DNA · protein are caused by histone fractions dissociated in the range of 0.7–1.0 M NaCl.
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