[Secondary structure of the polyhedral protein of the nuclear polyhedrosis virus of Bombyx mori and some of its fragments].
The secondary structure of polyhedral protein of the nuclear polyhedrosis virus of Bombyx mori and some of its fragments has been investigated by circular dichroism and optical rotatory dispersion. It has been shown that the protein contains 6% alpha-helices and 26% beta-structures at pH 10.5. The conversion of beta-pleated sheets to alpha-helices after the treatment with sodium dodecyl sulfate was observed. A correlation between the number of alpha-helices in the fragment BrCN-V and its ability to aggregate in aqueous solutions was observed. It was suggested that the COOH-terminal region of polypeptide chain of polyhedral protein makes a considerable contribution to the aggregation of subunits of the polyhedral protein.
D000818:Animals; D012831:Bombyx; D002942:Circular Dichroism; D003488:Cyanogen Bromide; D007304:Insect Viruses / Q000032:analysis*; D046911:Macromolecular Substances; D009905:Optical Rotatory Dispersion; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D014764:Viral Proteins
D046911:Macromolecular Substances; D010446:Peptide Fragments; D014764:Viral Proteins; D003488:Cyanogen Bromide
Issledovanie vtorichnoĭ struktury belka tel vkliucheniĭ virusa iadernorgo polizdroza Bomby x mori i ego fragmentov.