Spin‐Label Study of Histone H1–DNA Interaction

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Abstract
Covalent spin-labeling of Lys and Arg residues in histone H1 under specified conditions allows the study of histone-DNA [isolated from calf thymus] interaction. When the labeled histone is free in solution, the ER spectrum is characteristic of a label moving in a viscous medium while the label becomes fully immobilized upon the interaction of histone and DNA. This property is used to study histone-DNA interactions under various conditions of ionic strength and thermal denaturation. Spin-label probes in the globular part of the molecule show no strong immobilization upon binding to linear DNA, suggesting a special mechanism for the binding of histone H1 to chromatin.