In Physiological Salt Conditions the Core Proteins of the Nucleosomes in Large Chromatin Fragments Denature at 73 °C and the DNA Unstacks at 85 °C
Open Access
- 1 April 1989
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 264 (11) , 6515-6519
- https://doi.org/10.1016/s0021-9258(18)83378-6
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Protein-dependent conformational behavior of DNA in chromatinBiochemistry, 1987
- Differential scanning calorimetry of nuclei reveals the loss of major structural features in chromatin by brief nuclease treatment.Proceedings of the National Academy of Sciences, 1985
- Coupled endo-exodeoxyribonuclease activity from Hela cell nuclei interacts with specific regions of the SV40 mini chromosomeBiochemical and Biophysical Research Communications, 1985
- Sodium butyrate induced structural changes in HeLa cell chromatinBiochemistry, 1982
- Stability of DNA in nucleosomes.Proceedings of the National Academy of Sciences, 1980
- Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin.The Journal of cell biology, 1979
- Thermal denaturation of nucleosomal core particlesNucleic Acids Research, 1978
- Conformational States of ChromatinCold Spring Harbor Symposia on Quantitative Biology, 1978
- Studies on the thermal denaturation of nucleohistonesJournal of Molecular Biology, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970