A turn propensity scale for transmembrane helices
A turn propensity scale for transmembrane helices
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DOI：
10.1006/jmbi.1999.2657
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发表时间：
1999-04-23
影响因子：
5.6
通讯作者：
von Heijne, G
中科院分区：
文献类型：
--
作者：
Monné, M;Hermansson, M;von Heijne, G
使用具有 40 个残基的疏水性跨膜片段的模型蛋白，我们测量了所有 20 种天然存在的氨基酸在置于疏水性片段中间时形成紧转的能力。发现跨膜螺旋的转向倾向与球状蛋白的转向倾向显着不同，并且在大多数情况下与残基的疏水性密切相关。转向倾向量表可用于改进当前的膜蛋白拓扑预测方法。 (C) 1999 年学术出版社。
Using a model protein with a 40 residue hydrophobic transmembrane segment, we have measured the ability of all the 20 naturally occurring amino acids to form a tight turn when placed in the middle of the hydrophobic segment. Turn propensities in a transmembrane helix are found to be markedly different from those of globular proteins, and in most cases correlate closely with the hydrophobicity of the residue. The turn propensity scale may be used to improve current methods for membrane protein topology prediction. (C) 1999 Academic Press.