根据氨基酸序列预测膜蛋白的构象。
The prediction of the conformation of membrane proteins from the sequence of amino acids.
作者信息
Green N M, Flanagan M T
出版信息
Biochem J. 1976 Mar 1;153(3):729-32. doi: 10.1042/bj1530729.
Abstract
The methods of Chou & Fasman [Biochemistry (1974) 13, 211-222, 222-245] and of Lim [J. Mol. Biol. (1974)88, 857-872, 873-894] for predicting secondary structure from amino acid sequence have been applied to five predominantly helical membrane-associated peptides. The predictions from the method of Lim (1974a,b) are consistent with the experimental observations, whereas those from Chou & Fasman (1974a,b), although not inconsistent with alpha-helix, favour a beta-structure for several very hydrophobic regions. The results may be rationalized in terms of the effect of the solvent on the conformation of a polypeptide.
摘要
周和法斯曼[《生物化学》（1974年）13卷，211 - 222页，222 - 245页]以及利姆[《分子生物学杂志》（1974年）88卷，857 - 872页，873 - 894页]从氨基酸序列预测二级结构的方法已应用于五条主要为螺旋结构的膜相关肽段。利姆（1974年a、b）方法的预测结果与实验观察结果一致，而周和法斯曼（1974年a、b）方法的预测结果，尽管与α - 螺旋并不矛盾，但对于几个非常疏水的区域却倾向于β - 结构。这些结果可以从溶剂对多肽构象的影响方面进行合理说明。
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