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首页> 外文期刊>Journal of Molecular Biology >The 'Two-state Folder' MerP Forms Partially Unfolded Structures that Show Temperature Dependent Hydrogen Exchange.
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The 'Two-state Folder' MerP Forms Partially Unfolded Structures that Show Temperature Dependent Hydrogen Exchange.

机译：“两态文件夹” MerP形成部分展开的结构，该结构显示出与温度有关的氢交换。

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摘要

We have analysed the folding energy landscape of the 72 amino acid protein MerP by monitoring native state hydrogen exchange as a function of temperature in the range of 7-55 degrees C. The temperature dependence of the hydrogen exchange has allowed us to determine DeltaG, DeltaH and DeltaC(p) values for the conformational processes that permit hydrogen exchange. When studied with the traditional probes, fluorescence and CD, MerP appears to behave as a typical two-state protein, but the results from the hydrogen exchange analysis reveal a much more complex energy landscape. Analysis at the individual amino acid level show that exchange is allowed from an ensemble of partially unfolded structures (i.e. intermediates) in which the stabilities at the amino acid level form a broad distribution throughout the protein. The formation of partially unfolded structures might contribute to the unusually slow folding of MerP.
机译：我们已经通过监测7-55摄氏度范围内的温度变化来监测原生态氢交换，从而分析了72个氨基酸蛋白MerP的折叠能态。氢交换的温度依赖性使我们能够确定DeltaG，DeltaH以及允许氢交换的构象过程的DeltaC（p）值。用传统的探针，荧光和CD进行研究时，MerP似乎表现为典型的两种状态的蛋白质，但是氢交换分析的结果显示出更为复杂的能量格局。在单个氨基酸水平上的分析表明，可以从部分未折叠结构（即中间体）的集合中进行交换，其中氨基酸水平上的稳定性在整个蛋白质中形成了广泛的分布。部分展开结构的形成可能会导致MerP异常缓慢的折叠。

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