Khrapunov S N, Protas A F, Berdyshev G D
Biofizika. 1984 Jul-Aug;29(4):590-4.
In the region of 50 mM NaCl histone HI has the structure with a great number of binding sites with fluorescent probe 1.8-ANS as compared to the structure formed in solution of 0.6-1.0 M NaCl. These sites, however, have a lower constant of binding with the probe and are characterized by a higher surrounding polarity. At local significant increase of the ionic strength histone HI molecules form stable oligomers having hydrophobic cavities. A conclusion is made about the importance of cationic envelope formed by N- and C-ends around the globular "head", for manifesting effective interactions between several molecules of histone HI.
在50 mM NaCl浓度区域，与在0.6 - 1.0 M NaCl溶液中形成的结构相比，组蛋白H1具有大量与荧光探针1.8 - ANS结合的位点。然而，这些位点与探针的结合常数较低，且其周围极性较高。当离子强度局部显著增加时，组蛋白H1分子形成具有疏水腔的稳定寡聚体。得出这样的结论：由N端和C端围绕球状“头部”形成的阳离子包膜，对于组蛋白H1的几个分子之间表现出有效的相互作用至关重要。
