title: Proteolytic dissection of Sindbis virus core protein.
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.
authors.affiliation: Harvard University, Cambridge, Massachusetts.
authors.forename: R K
authors.initials: RK
authors.lastname: Strong
authors.forename: S C
authors.initials: SC
authors.lastname: Harrison
mesh_terms: D002213:Capsid / Q000302:isolation & purification; D002850:Chromatography, Gel; D007700:Kinetics; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D010449:Peptide Mapping; D012845:Sindbis Virus / Q000032:analysis*; D014357:Trypsin / Q000378:metabolism; D014758:Viral Core Proteins / Q000302:isolation & purification
chemical_list: D010446:Peptide Fragments; D014758:Viral Core Proteins; D014357:Trypsin