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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR
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Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR

机译：超快H / D交换结合2D NMR揭示了肌红蛋白的分层折叠机制

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摘要

The earliest steps in the folding of proteins are complete on an extremely rapid time scale that is difficult to access experimentally. We have used rapid-mixing quench-flow methods to extend the time resolution of folding studies on apomyoglobin and elucidate the structural and dynamic features of members of the ensemble of intermediate states that are populated on a submillisecond time scale during this process. The picture that emerges is of a continuum of rapidly interconverting states. Even after only 0.4 ms of refolding time a compact state is formed that contains major parts of the A, G, and H helices, which are sufficiently well folded to protect amides from exchange. The B, C, and E helix regions fold more slowly and fluctuate rapidly between open and closed states as they search docking sites on this core; the secondary structure in these regions becomes stabilized as the refolding time is increased from 0.4 to 6 ms. No further stabilization occurs in the A, G, H core at 6 ms of folding time. These studies begin to time-resolve a progression of compact states between the fully unfolded and native folded states and confirm the presence an ensemble of intermediates that interconvert in a hierarchical sequence as the protein searches conformational space on its folding trajectory.
机译：蛋白质折叠的最早步骤是在极快的时间范围内完成的，很难通过实验获得。我们已经使用快速混合淬灭流方法来扩展对apglooglobin的折叠研究的时间分辨率，并阐明在此过程中以亚毫秒级为单位的中间状态集合体的结构和动态特征。出现的画面是快速相互转换状态的连续体。即使在仅0.4 ms的重折叠时间后，仍会形成包含A，G和H螺旋主要部分的紧凑状态，这些部分折叠得足够好以保护酰胺不被交换。当B，C和E螺旋区域搜索该核心上的对接位点时，它们在打开状态和关闭状态之间的折叠速度较慢，并迅速波动。随着重新折叠时间从0.4毫秒增加到6毫秒，这些区域的二级结构变得稳定。折叠时间为6 ms时，A，G，H磁芯中没有进一步的稳定作用。这些研究开始时间解析紧密状态在完全展开状态和天然折叠状态之间的进展，并确认存在中间体的集合，这些中间体在蛋白质搜索其折叠轨迹上的构象空间时以分层序列相互转换。

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