Amino-terminal sequence analysis of the structural proteins of Sindbis virus.

Abstract
The structural proteins of Sindbis virus, an enveloped virus which belongs to the Togavirus family, were subjected to automated Edman degradation using improved techniques. Extensive NH2-terminal sequences of about 50 residues were determined for each of the 2 membrane glycoproteins. In both cases the NH2 terminus of the molecule was similar in composition to typical water-soluble proteins. The viral capsid protein had a blocked .alpha.-amino group. This is consistent with other observations that viral proteins derived from the NH2 terminus of precursor molecules are often blocked.