The dependence of the proton spin-lattice relaxation rate, and of the enthalpy and temperature of denaturation on water content, were studied by nmr and differential scanning calorimetry (DSC) in native and denatured collagen. Collagen was first heated at four different temperatures ranging from 40
H2B nucleohistone — phospholipid interactions. Thermal denaturation and ultrastructural analysis
✍ Scribed by S. Capitani; N. M. Maraldi; L. Cocco; P. Santi; F. A. Manzoli
- Book ID
- 104679886
- Publisher
- Springer
- Year
- 1978
- Tongue
- English
- Weight
- 636 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0300-8177
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✦ Synopsis
Sphingomyelin, phosphatidylserine, bovine lecithin and phosphatidylethanolamine modify the thermal stabilization of H2B-DNA complexes, by inducing stabilization at 0.3 and 0.6 H2B : DNA weight ratios and destabilify the arrangement of nucleohistone is confirmed by ultrastructural analysis which indicates a competitive action of these molecules during the nucleoprotein assembly. A possible regulatory role of phospholipids on native chromatin is proposed.
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