Driving forces for transmembrane alpha-helix oligomerization.
Driving forces for transmembrane alpha-helix oligomerization.
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跨膜α螺旋寡聚的驱动力。
DOI：
10.1016/j.bpj.2010.03.071
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发表时间：
2010
影响因子：
3.4
通讯作者：
Head-Gordon,Teresa
中科院分区：
文献类型：
--
作者：
Sodt,AlexJ;Head-Gordon,Teresa
我们提出了我们认为是一种新的统计接触电位的基础上解决跨膜（TM）α-螺旋束的结构，我们使用这种接触电位来研究稳定螺旋-螺旋界面的氨基酸的可能性。为了增加统计学意义，我们已经减少了完整的接触能矩阵的氨基酸，自动确定我们的方法，其中我们发现，极性是一个更占主导地位的因素组身份比大小，带电或极性基团最经常占据同一面，而极性/非极性残基对往往占据相反的面。我们发现，最极性的残基强烈影响螺旋间接触的形成，虽然他们很少发生在TM螺旋束。在减少字母代码中的两体接触能能够从大多数测试TM蛋白的大诱饵集确定天然结构，同时说明某些高阶序列相关性对于更准确的结构预测是必要的。
We present what we believe to be a novel statistical contact potential based on solved structures of transmembrane (TM)α-helical bundles, and we use this contact potential to investigate the amino acid likelihood of stabilizing helix-helix interfaces. To increase statistical significance, we have reduced the full contact energy matrix to a four-flavor alphabet of amino acids, automatically determined by our methodology, in which we find that polarity is a more dominant factor of group identity than is size, with charged or polar groups most often occupying the same face, whereas polar/apolar residue pairs tend to occupy opposite faces. We found that the most polar residues strongly influence interhelical contact formation, although they occur rarely in TM helical bundles. Two-body contact energies in the reduced letter code are capable of determining native structure from a large decoy set for a majority of test TM proteins, at the same time illustrating that certain higher-order sequence correlations are necessary for more accurate structure predictions.