1.
Mol Biol (Mosk)
; 10(2): 514-20, 1976.
Artigo
em Russo
| MEDLINE
| ID: mdl-1053037
RESUMO
Characteristic viscosity, sedimentation constant and optical anisotropy were studied of the complexes formed between DNA and histone fractions F3 and F3+F2a2. The parameters mentioned continuously change with the increase of protein content within the complex. Analysis of experimental data shows that binding of a histone bads to a decrease of size and thermodynamic rigidity of the DNA molecule. On the basis of results obtained a model of F3 histone binding with DNA is suggested, amino acid sequence of this protein being taken into account. Comparison of behaviour of nucleohistones DNA+F3 and DNA+F1 studied previously testifies different way of binding of these histones to DNA.
Assuntos
DNA , Desoxirribonucleoproteínas , Histonas , Nucleoproteínas , Cinética , Conformação de Ácido Nucleico , Conformação Proteica , Termodinâmica , Viscosidade
2.
Mol Biol
; 7(5): 614-20, 1974 Mar.
Artigo
em Inglês
| MEDLINE
| ID: mdl-4825848
3.
Biorheology
; 10(1): 7-16, 1973 Mar.
Artigo
em Inglês
| MEDLINE
| ID: mdl-4724182