Abstract
Predictions of secondary structure for the 2 chains HA1 and HA2 of the hemagglutinin from the Hong Kong influenza virus A/Memphis/102/72 reveal a striking contrast between the potential conformations of the 2 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 hemagglutinin monomers together in the virus.