Kibirev V K, Radavskiĭ Iu L, Sukhareiko N V, Serebrianyĭ S B
Mol Biol (Mosk). 1976 Nov-Dec;10(6):1272-8.
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.
利用圆二色性和旋光色散对家蚕核型多角体病毒多面体蛋白及其一些片段的二级结构进行了研究。结果表明，在pH 10.5时，该蛋白含有6%的α-螺旋和26%的β-结构。观察到用十二烷基硫酸钠处理后β-折叠片层向α-螺旋的转变。观察到片段BrCN-V中α-螺旋的数量与其在水溶液中聚集能力之间的相关性。有人提出，多面体蛋白多肽链的COOH末端区域对多面体蛋白亚基的聚集有相当大的贡献。
