Structural prediction of membrane-bound proteins.
Structural prediction of membrane-bound proteins.
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DOI：
10.1111/j.1432-1033.1982.tb07002.x
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发表时间：
2005-03
期刊：
影响因子：
--
通讯作者：
P. Argos;J. K. M. Rao;P. Hargrave
中科院分区：
文献类型：
--
作者：
P. Argos;J. K. M. Rao;P. Hargrave
一个预测算法的基础上的20个氨基酸的物理特性和完善的建议细菌视紫红质结构的比较被设计来描绘可能的膜埋在已知的蛋白质与脂质双层的主要序列的区域。应用该方法的序列的羧基末端三分之一的牛视紫红质预测膜埋螺旋发夹结构。利用细菌视紫红质中的脂质埋藏片段以及其他膜结合蛋白中的算法预测的区域，计算了20种氨基酸在其偏好中与脂质接触的分级排序。预测区域的螺旋轮分析表明，哪些螺旋面在蛋白质内部，哪些与脂质双层接触。
A prediction algorithm based on physical characteristics of the twenty amino acids and refined by comparison to the proposed bacteriorhodopsin structure was devised to delineate likely membrane-buried regions in the primary sequences of proteins known to interact with the lipid bilayer. Application of the method to the sequence of the carboxyl terminal one-third of bovine rhodopsin predicted a membrane-buried helical hairpin structure. With the use of lipid-buried segments in bacteriorhodopsin as well as regions predicted by the algorithm in other membrane-bound proteins, a hierarchical ranking of the twenty amino acids in their preferences to be in lipid contact was calculated. A helical wheel analysis of the predicted regions suggests which helical faces are within the protein interior and which are in contact with the lipid bilayer.