Reports

Histone Structure: Asymmetric Distribution of Lysine Residues in Lysine-rich Histone

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Science  24 Jan 1969:
Vol. 163, Issue 3865, pp. 391-393
DOI: 10.1126/science.163.3865.391-a

Abstract

Structural studies on a very lysine-rich histone show that the carboxyl-terminal half of the molecule is enriched in lysine (and proline). which suggests that it is a site for binding to DNA. The amino-terminal half. containing most of the acidic residues. resembles small, nonhistone proteins and so might have specificity for factors other than DNA.

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