GB1 Is Not a Two-State Folder: Identification and Characterization of an On-Pathway Intermediate
GB1 Is Not a Two-State Folder: Identification and Characterization of an On-Pathway Intermediate
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DOI：
10.1016/j.bpj.2011.09.013
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发表时间：
2011-10-19
影响因子：
3.4
通讯作者：
Gianni, Stefano
中科院分区：
文献类型：
--
作者：
Morrone, Angela;Giri, Rajanish;Gianni, Stefano
在过去的二十年里，人们利用理论和实验方法对小 α/β 蛋白 GB1 的折叠途径进行了广泛的研究。这些研究提供了一个共识，即蛋白质以两种状态方式折叠。在这里，我们通过实验和模拟重新评估了 GB1 的折叠，并检测到了路径上中间体的存在。这种中间体避开了早期的实验表征，并且与之前使用超快速混合识别的塌缩状态不同。未能确定中间体的存在会影响 GB1（蛋白质折叠研究的流行模型）得出的一些结论。
The folding pathway of the small alpha/beta protein GB1 has been extensively studied during the past two decades using both theoretical and experimental approaches. These studies provided a consensus view that the protein folds in a two-state manner. Here, we reassessed the folding of GB1, both by experiments and simulations, and detected the presence of an on-pathway intermediate. This intermediate has eluded earlier experimental characterization and is distinct from the collapsed state previously identified using ultrarapid mixing. Failure to identify the presence of an intermediate affects some of the conclusions that have been drawn for GB1, a popular model for protein folding studies.