Siniakov M S, Kharitonenkov I G
Vopr Virusol. 1980 Jan-Feb(1):45-9.
The method of circular dichroism was used to evaluate the conformation parameters of the secondary structure of the molecule of isolated influenza virus hemagglutinin H3. Comparison of the data obtained with the similar known parameters for hemagglutinin H2 has shown significant differences in the secondary structure, which are, probably, responsible, (at the level of a higher structural organization) for the variations in the antigenic specificity of hemagglutinins H2 and H3. Temperature and pH stability of alpha-spiral areas of the hemagglutinin H3 molecule was studied, and the direct participation of aromatic amino acid residues in formation of the alpha-spiral areas was shown. The native state of the hemagglutinin alpha-spiral areas may serve as a factor determining potential hemagglutination.
采用圆二色性方法评估分离出的流感病毒血凝素H3分子二级结构的构象参数。将所得数据与血凝素H2的类似已知参数进行比较，结果表明二级结构存在显著差异，这可能（在更高结构组织水平上）导致了血凝素H2和H3抗原特异性的变化。研究了血凝素H3分子α-螺旋区域的温度和pH稳定性，并证明了芳香族氨基酸残基直接参与α-螺旋区域的形成。血凝素α-螺旋区域的天然状态可能是决定潜在血凝作用的一个因素。
