Ward C W, Dopheide T A
Aust J Biol Sci. 1980 Aug;33(4):441-7. doi: 10.1071/bi9800441.
Predictions of secondary structure for the two chains HA1 and HA2 of the haemagglutinin from the Hong Kong influenza virus A/Memphis/102/72 reveal a striking contrast between the potential conformations of the two chains. HA1 is predicted to be rich in beta-structure while HA2 is highly helical. The predictions further suggest that coiled-coil type interactions between the central helical segments of the HA2 chains may hold the haemagglutinin monomers together in the virus.
对香港甲型流感病毒A/孟菲斯/102/72血凝素的两条链HA1和HA2二级结构的预测显示，两条链的潜在构象之间存在显著差异。预测HA1富含β结构，而HA2则高度螺旋化。这些预测进一步表明，HA2链中央螺旋段之间的卷曲螺旋型相互作用可能将血凝素单体在病毒中结合在一起。
