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The hydrophobic interaction between histone H1 and DNA appears to be an important mechanism of gene regulation in chromatin structure. A series of H1-DNA complexes with different proportions of protein and nucleic acid (DNA) have been studied by difference spectroscopy and 13C relaxation time experiments. The magnitude of negative absorption in the difference spectrum of H1-DNA complexes decreases with increasing molar DNA:protein ratio. This means that with increasing molar ratio the protein-DNA interaction in the complex changes from hydrophobic to a combination of hydrophobic and electrostatic interactions. This is supported by electron microscopy and gel electrophoresis results. It is concluded that at low protein concentrations DNA is associated with proteins predominantly through hydrophobic forces, whereas at higher concentrations more electrostatic interactions also contribute to the binding. The 13C relaxation time measurements of 13C-labeled H1-DNA complexes with a range of DNA:protein ratios show that a third fraction of the DNA in the complex is characterized by a very long relaxation time. This may represent a polymerized fraction of the DNA in the complex.What does a writer do when he writes? Think of all the things he doesn’t do. Sitting at his desk, working the editor’s keyboard, he doesn’t say, “Can you describe this in short, concise sentences?” No, he doesn’t say, “Read what I’ve written, and tell me what you think.” He doesn’t think at all. He is absorbed in creating things, or doing things, or calling things into being. The ink is flowing
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