Shestopalov B V, Chirgadze Y N
Eur J Biochem. 1976 Aug 1;67(1):123-8. doi: 10.1111/j.1432-1033.1976.tb10640.x.
The secondary structure of histones H1, H2A, and H4 (F1, F2a2, and F2a1) has been quantitatively studied in heavy water (2H2O) solutions in a wide range of histone concentration, p2H, and concentration of sodium chloride using an improved infrared spectroscopy method. Under all conditions there are about 5--10% of alpha helix. Conditions favourable for aggregation induce formation of antiparallel pleated sheet structure to an extent of about 15% in H1 and H2A and about 30% in H4. When the p2H and concentration of NaCl are in the physiological range, there is the same content of this structure in H2A and H4 and none in H1.
使用改进的红外光谱法，在重水（2H₂O）溶液中，于广泛的组蛋白浓度、p2H值和氯化钠浓度范围内，对组蛋白H1、H2A和H4（F1、F2a2和F2a1）的二级结构进行了定量研究。在所有条件下，约有5%-10%的α螺旋。有利于聚集的条件会诱导反平行β折叠片层结构的形成，在H1和H2A中约占15%，在H4中约占30%。当p2H值和氯化钠浓度处于生理范围内时，H2A和H4中该结构的含量相同，而H1中则没有。
