Membrane protein folding: how important are hydrogen bonds?
Membrane protein folding: how important are hydrogen bonds?
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DOI：
10.1016/j.sbi.2010.10.003
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发表时间：
2011-02
影响因子：
6.8
通讯作者：
Bowie, James U.
中科院分区：
文献类型：
--
作者：
Bowie, James U.
水是一个不适合蛋白质氢键的环境，因为它是可极化的，能够形成竞争性氢键。相比之下，生物膜的非极性核心似乎是氢键的理想环境，长期以来人们一直认为氢键应该是驱动膜蛋白折叠的强大力量。然而，虽然骨架氢键可能是强得多的膜蛋白，实验测量表明，侧链氢键的强度并没有显着不同的膜和水溶性蛋白质。这怎么可能？我认为，模型化合物在非极性溶剂不充分描述系统，因为蛋白质本身被忽略。蛋白质链提供了丰富的竞争性氢键来源和可削弱氢键的可极化环境。因此，就像水溶性蛋白质一样，进化可以在必要时驱动膜蛋白质中产生有效的氢键，但仍必须克服其环境中的缓解力。
Water is an inhospitable environment for protein hydrogen bonds because it is polarizable and capable of forming competitive hydrogen bonds. In contrast, the apolar core of a biological membrane seems like an ideal environment for hydrogen bonds, and it has long been assumed that hydrogen bonding should be a powerful force driving membrane protein folding. Nevertheless, while backbone hydrogen bonds may be much stronger in membrane proteins, experimental measurements indicate that side chain hydrogen bond strengths are not strikingly different in membrane and water soluble proteins. How is this possible? I argue that that model compounds in apolar solvents do not adequately describe the system because the protein itself is ignored. The protein chain provides a rich source of competitive hydrogen bonds and a polarizable environment that can weaken hydrogen bonds. Thus, just like water soluble proteins, evolution can drive the creation of potent hydrogen bonds in membrane proteins where necessary, but mitigating forces in their environment must still be overcome.
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影响因子：
3.4
作者：
Chamberlain, AK;Bowie, JU
通讯作者：
Bowie, JU
影响因子：
5.6
作者：
Dawson, JP;Weinger, JS;Engelman, DM
通讯作者：
Engelman, DM
影响因子：
2.9
作者：
Goch, G;Maciejczyk, M;Bierzynski, A
通讯作者：
Bierzynski, A
DOI：
10.1038/72454
发表时间：
2000-02-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
--
作者：
Bowie, JU
通讯作者：
Bowie, JU
影响因子：
15
作者：
Arbely, E;Arkin, IT
通讯作者：
Arkin, IT