Abstract
The S2 subunit of the spike glycoprotein from SARS coronavirus (CoV) contains internal membranotropic domains that play important roles to the viral and host cell membrane fusion. These functional domains, which include a so-called fusion peptide (FP) and an internal FP, are exposed to membrane interactions upon a specific trigger. Although membrane fusion has been broadly studied in recent years, many aspects of the molecular mechanism behind the virus-host cell membrane fusion remain unknown, including conformational changes of the lipid bilayers during peptide-membrane interactions.
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