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