Histone structure: asymmetric distribution of lysine residues in lysine-rich histone.
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.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002850:Chromatography, Gel; D002918:Chymotrypsin; D004247:DNA; D006657:Histones / Q000032:analysis*; D008239:Lysine / Q000032:analysis*; D010455:Peptides / Q000032:analysis*; D011760:Pyrrolidinones; D013950:Thymus Gland
D006657:Histones; D010455:Peptides; D011760:Pyrrolidinones; D004247:DNA; D002918:Chymotrypsin; D008239:Lysine