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Journal of Virology logoLink to Journal of Virology
. 1990 Aug;64(8):3992–3994. doi: 10.1128/jvi.64.8.3992-3994.1990

Proteolytic dissection of Sindbis virus core protein.

R K Strong 1, S C Harrison 1
PMCID: PMC249698  PMID: 2370686

Abstract

Mild trypsin treatment of the Sindbis virus nucleocapsid protein yields a fragment with a molecular mass of approximately 18.5 kilodaltons with its N terminus at residue 105. The fragment, which is stable to further digestion, appears by gel exclusion chromatography to be monomeric. These data are consistent with a model for the alphavirus core proteins, consisting of an extended and flexible N-terminal arm (residues 1 to 103) and a compactly folded C-terminal domain (residues 104 to 274), as previously suggested on the basis of sequence characteristics.

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Selected References

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