Snorkeling preferences foster an amino acid composition bias in transmembrane helices
Snorkeling preferences foster an amino acid composition bias in transmembrane helices
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DOI：
10.1016/j.jmb.2004.03.072
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发表时间：
2004-05-28
影响因子：
5.6
通讯作者：
Bowie, JU
中科院分区：
文献类型：
--
作者：
Chamberlain, AK;Lee, Y;Bowie, JU
通过分析已知结构中的跨膜（TM）螺旋，我们发现一些极性氨基酸在N末端比在C末端更常见。我们认为，不对称的发生是因为大多数极性氨基酸能够更好地从N端比在C端的膜核心浮潜其极性原子。两个发现使我们得出这个结论：（1）侧链构象受到双层中氨基酸的N或C末端位置的强烈影响，（2）氨基酸的有利浮潜方向与其N至C末端组成偏好密切相关。我们的研究结果表明，TM螺旋预测应纳入N-C-末端组成的偏见，旋转异构体的TM侧链的偏好是位置依赖性的，和通气管的能力影响的进化选择的螺旋N和C末端的氨基酸。(C)2004爱思唯尔有限公司保留所有权利。
By analyzing transmembrane (TM) helices in known structures, we find that some polar amino acids are more frequent at the N terminus than at the C terminus. We propose the asymmetry occurs because most polar amino acids are better able to snorkel their polar atoms away from the membrane core at the N terminus than at the C terminus. Two findings lead us to this proposition: (1) side-chain conformations are influenced strongly by the N or C-terminal position of the amino acid in the bilayer, and (2) the favored snorkeling direction of an amino acid correlates well with its N to C-terminal composition bias. Our results suggest that TM helix predictions should incorporate an N to C-terminal composition bias, that rotamer preferences of TM side-chains are position-dependent, and that the ability to snorkel influences the evolutionary selection of amino acids for the helix N and C termini. (C) 2004 Elsevier Ltd. All rights reserved.