Hamodrakas S J, Batrinou A, Christophoratou T
Department of Biochemistry, Cell and Molecular Biology and Genetics, University of Athens, Greece.
Int J Biol Macromol. 1989 Oct;11(5):307-13. doi: 10.1016/0141-8130(89)90025-1.
Amino acid composition, Fourier transform analysis and secondary structure prediction methods strongly support a tripartite structure for Drosophila chorion proteins s36 and s38. Each protein consists of a central domain and two flanking 'arms'. The central domain contains tandemly repetitive peptides, which apparently generate a secondary structure of beta-sheet strands alternating with beta-turns, most probably, forming a twisted beta-pleated sheet or beta-barrel. The central domains of s36 and s38 share similarities, but they are recognizably different. The flanking 'arms', with different primary and secondary structure features, presumably serve protein-specific functions. The possible roles of the protein domains for the establishment of higher order structure in Drosophila chorion and the possible function of the molecules are discussed. The predicted secondary structure of Drosophila chorion proteins s36 and s38 is supported by experimental information obtained from Fourier transform infrared spectroscopic studies of Drosophila chorions.
氨基酸组成、傅里叶变换分析和二级结构预测方法有力地支持了果蝇绒毛膜蛋白s36和s38的三方结构。每种蛋白质都由一个中央结构域和两个侧翼“臂”组成。中央结构域包含串联重复肽段，这些肽段显然会产生β-折叠链与β-转角交替的二级结构，很可能形成扭曲的β-折叠片层或β-桶状结构。s36和s38的中央结构域有相似之处，但也有明显差异。侧翼“臂”具有不同的一级和二级结构特征，可能发挥蛋白质特异性功能。文中讨论了蛋白质结构域在果蝇绒毛膜中形成高阶结构的可能作用以及这些分子的可能功能。果蝇绒毛膜蛋白s36和s38的预测二级结构得到了从果蝇绒毛膜的傅里叶变换红外光谱研究中获得的实验信息的支持。
