## Abstract The conformation of deoxyribonucleoprotein (DNP) from calf thymus at different stages of deproteinization was studied. The dissociation of the first portion of histone produces no effect on the hydrodynamical and optical behavior of DNP particles. The conformational transition of a mac
Collapse of extended deoxyribonucleoprotein molecules upon increase of the ionic strength of solution
β Scribed by A.Ya. Varshavsky; Yu.V. Ilyin; V.I. Kadyckov; E.P. Senchenkov
- Book ID
- 115744604
- Publisher
- Elsevier Science
- Year
- 1971
- Weight
- 832 KB
- Volume
- 246
- Category
- Article
- ISSN
- 0005-2787
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Increasing the ionic strength of rat liver chromatin solutions above 0.4 M causes increasing viscosity. This indicates transformation of the compact chromatin molecules to more elongated forms. In the range of 0.4-0.5 M ionic strength histone H1 is dissociating continuously from the chromatin and th
## Abstract The crossβsectional radius of gyration of the deoxyribonucleoprotein (DNP) threads was measured by smallβangle Xβray scattering in a wide range of ionic strengths (from 0.0005 to 2 __M__ NaCl). For DNP in a solution of low ionic strength, this value is 30 Γ . The increase of ionic streng