Influenza virus hemagglutinin H3: Conformation in solution

M. S. Sinyakov, I. G. Kharitonenkov

Research output: Contribution to journalArticlepeer-review


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 α-spiral areas of the hemagglutinin H3 molecule was studied, and the direct participation of aromatic amino acid residues in formation of the α-spiral areas was shown. The native state of the hemagglutinin α-spiral areas may serve as a factor determining potential hemaglutination.

Original languageEnglish
Pages (from-to)45-49
Number of pages5
JournalVoprosy Virusologii
Issue number1
StatePublished - 1980
Externally publishedYes


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