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Histone structure: asymmetric distribution of lysine residues in lysine-rich histone.
Science ; 163(3865): 391-3, 1969 Jan 24.
Article in En | MEDLINE | ID: mdl-5762775
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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Collection: 01-internacional Database: MEDLINE Main subject: Peptides / Histones / Amino Acid Sequence / Lysine Limits: Animals Language: En Journal: Science Year: 1969 Type: Article
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Peptides / Histones / Amino Acid Sequence / Lysine Limits: Animals Language: En Journal: Science Year: 1969 Type: Article