Nucleosomal subunits isolated from rabbit thymus nuclei in 0.04 M K2SO 4-0.02 M Tris, pH 7.4 were devoid of histone H1, while whole chromatin prepared in the same buffer contained the full complement of histone HI. The question is asked why histone H1 dissociates from the subunits but not from the h
β¦ LIBER β¦
Binding of additional histones to chromatin core particles
β Scribed by Voordouw, Gerrit; Eisenberg, Henryk
- Book ID
- 109709705
- Publisher
- Nature Publishing Group
- Year
- 1978
- Tongue
- English
- Weight
- 356 KB
- Volume
- 273
- Category
- Article
- ISSN
- 0028-0836
- DOI
- 10.1038/273446a0
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
On the binding of histone H1 in chromati
β
Robert C. Krueger
π
Article
π
1986
π
Springer
π
English
β 448 KB
Determinants of histone H1 mobility and
β
Catez, FrΓ©dΓ©ric; Ueda, Tetsuya; Bustin, Michael
π
Article
π
2006
π
Nature Publishing Group
π
English
β 315 KB
31P magnetic resonance of DNA in nucleos
β
Kallenbach, N. R.; Appleby, D. W.; Bradley, C. H.
π
Article
π
1978
π
Nature Publishing Group
π
English
β 595 KB
Regulation of HP1βchromatin binding by h
β
Fischle, Wolfgang; Tseng, Boo Shan; Dormann, Holger L.; Ueberheide, Beatrix M.;
π
Article
π
2005
π
Nature Publishing Group
π
English
β 878 KB
Neutron-scattering studies of the struct
β
Gordon W. Braddock; John P. Baldwin; E. Morton Bradbury
π
Article
π
1981
π
Wiley (John Wiley & Sons)
π
English
β 894 KB
## Abstract The structure of the nucleosome core particle in solution has been studied by neutron scattering using the fullβcontrast variation technique, which reduces the experimental spectra to three fundamental scatter functions holding information on shape and structure. Systematic calculations
Modification of the lysine residues of h
β
J. Jordano; J. L. Barbero; F. Montero; E. PalaciΓ‘n
π
Article
π
1985
π
Springer
π
English
β 316 KB