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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Snapshots of a protein folding intermediate
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Snapshots of a protein folding intermediate

机译：蛋白质折叠中间体的快照

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We have investigated the folding dynamics of Thermus thermo-philus cytochrome c_(552) by time-resolved fluorescence energy transfer between the heme and each of seven site-specific fluorescent probes. We have found both an equilibrium unfolding intermediate and a distinct refolding intermediate from kinetics studies. Depending on the protein region monitored, we observed either two-state or three-state denaturation transitions. The unfolding intermediate associated with three-state folding exhibited native contacts in β-sheet and C-terminal helix regions. We probed the formation of a refolding intermediate by time-resolved fluorescence energy transfer between residue 110 and the heme using a continuous flow mixer. The intermediate ensemble, a heterogeneous mixture of compact and extended polypeptides, forms in a millisecond, substantially slower than the ～100-μs formation of a burst-phase intermediate in cytochrome c. The surprising finding is that, unlike for cytochrome c, there is an observable folding intermediate, but no microsecond burst phase in the folding kinetics of the structurally related thermostable protein.
机译：我们已经研究了血红素与七个特定位点荧光探针之间的时间分辨荧光能量转移，从而研究了嗜热栖热菌细胞色素c_（552）的折叠动力学。我们已经从动力学研究中发现了一个平衡的展开中间体和一个独特的重折叠中间体。根据所监测的蛋白质区域，我们观察到两个或三个状态的变性转变。与三态折叠有关的未折叠中间体在β-折叠和C-末端螺旋区域中表现出天然接触。我们通过使用连续流动混合器在残留物110和血红素之间进行时间分辨的荧光能量转移来探测重折叠中间体的形成。中间体集合体是紧实多肽和扩展多肽的异质混合物，形成时间为一毫秒，比细胞色素c中爆发相中间体的约100-μs形成要慢得多。令人惊讶的发现是，与细胞色素c不同，在结构相关的热稳定蛋白的折叠动力学中存在可观察到的折叠中间体，但没有微秒的爆发期。

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