Denesyuk A I, Zav'yalov V P
Immunol Lett. 1982 Oct;5(4):223-6. doi: 10.1016/0165-2478(82)90139-0.
Using the method of estimation of alpha-helical and beta-folded types of secondary structure from amino acid composition, it has been established that interferon-gamma (IFN-gamma) contains about 50-70% of alpha-helical and no more than 10-20% of beta-structure. The same result was obtained using empirical and stereochemical rules for the prediction of protein secondary structure from amino acid sequence. Packing of alpha-helical segments of IFN-gamma into 1 of the 2 three-dimensional structures previously suggested for IFN-alpha and IFN-beta, allowed to detect high conservativity of the hydrophobic core of the proteins compared. On this basis a tentative conclusion has been drawn that all interferons have, in general features, a similar globular alpha-helical conformation.
使用从氨基酸组成估计二级结构的α-螺旋和β-折叠类型的方法，已确定γ-干扰素（IFN-γ）含有约50-70%的α-螺旋，且β-结构不超过10-20%。使用从氨基酸序列预测蛋白质二级结构的经验规则和立体化学规则也得到了相同的结果。将IFN-γ的α-螺旋片段组装到先前为IFN-α和IFN-β提出的两种三维结构之一中，使得能够检测到所比较蛋白质疏水核心的高度保守性。在此基础上得出了一个初步结论，即所有干扰素在总体特征上具有相似的球状α-螺旋构象。
