Fast slow folding of an outer membrane porin.
Fast slow folding of an outer membrane porin.
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DOI：
10.1073/pnas.2121487119
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发表时间：
2022-05-17
影响因子：
11.1
通讯作者：
中科院分区：
文献类型：
--
作者：
外膜孔蛋白在能量产生、光合作用和营养物质运输等多种过程中起着至关重要的作用。它们是革兰氏阴性细菌与其环境之间的守门人。了解这些蛋白质的折叠和功能对于提高我们对这些过程的理解和控制非常重要。在这里，我们使用单分子方法来帮助解决在分子尺度上预期的快速折叠和在实验室中观察到的系综测量中的慢动力学之间的明显差异。与球状蛋白相比，β桶膜蛋白的自发折叠和插入异常缓慢，通常发生在几分钟左右。利用单分子Förster共振能量转移报道荧光标记的外膜蛋白G的折叠，我们测量了β桶膜蛋白从未折叠状态的实时插入。折叠事件罕见且快速（<20 ms），在到达膜后立即发生。这种不频繁但快速的折叠组合解决了缓慢集合动力学和典型生物分子折叠时间尺度之间的明显二分法。
Outer membrane porins play a crucial role in processes as varied as energy production, photosynthesis, and nutrient transport. They act as the gatekeepers between a gram-negative bacterium and its environment. Understanding how these proteins fold and function is important in improving our understanding and control of these processes. Here we use single-molecule methods to help resolve the apparent differences between the fast folding expected on a molecular scale and the slow kinetics observed in ensemble measurements in the laboratory. In comparison to globular proteins, the spontaneous folding and insertion of β-barrel membrane proteins are surprisingly slow, typically occurring on the order of minutes. Using single-molecule Förster resonance energy transfer to report on the folding of fluorescently labeled outer membrane protein G we measured the real-time insertion of a β-barrel membrane protein from an unfolded state. Folding events were rare and fast (<20 ms), occurring immediately upon arrival at the membrane. This combination of infrequent, but rapid, folding resolves this apparent dichotomy between slow ensemble kinetics and the typical timescales of biomolecular folding.
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影响因子：
--
作者：
Bayley H;Cronin B;Heron A;Holden MA;Hwang WL;Syeda R;Thompson J;Wallace M
通讯作者：
Wallace M
影响因子：
4.8
作者：
Doerrler, WT;Raetz, CRH
通讯作者：
Raetz, CRH
影响因子：
3.9
作者：
Ghai I;Ghai S
通讯作者：
Ghai S
DOI：
10.1073/pnas.0711561105
发表时间：
2008-04-29
影响因子：
11.1
作者：
Chen, Min;Khalid, Syma;Bayley, Hagan
通讯作者：
Bayley, Hagan
影响因子：
3.2
作者：
BLOCH, MA;DESAYMARD, C
通讯作者：
DESAYMARD, C