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Product Description
The capsid protein of Nudaurelia capensis ω Virus (NωV) has previously been characterized in two dramatically different T = 4 quasi-equivalent assembly states when expressed as virus-like particles (VLPs) in a baculovirus system. The procapsid (pH 7), is round, porous, and approximately 450 Å in diameter. It converts, in vitro, to the capsid form at pH 5 and the capsid is sealed shut, shaped like an icosahedron, has a maximum diameter of 410 Å and undergoes an autocatalytic cleavage at residue 570.