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首页> 外文期刊>Journal of Molecular Biology >The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms.
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The folding trajectory of RNase H is dominated by its topology and not local stability: a protein engineering study of variants that fold via two-state and three-state mechanisms.

机译：RNase H的折叠轨迹主要受其拓扑结构而不是局部稳定性的影响：一项蛋白质工程研究，研究了通过二态和三态机制折叠的变异体。

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摘要

Proteins can sample a variety of partially folded conformations during the transition between the unfolded and native states. Some proteins never significantly populate these high-energy states and fold by an apparently two-state process. However, many proteins populate detectable, partially folded forms during the folding process. The role of such intermediates is a matter of considerable debate. A single amino acid change can convert Escherichia coli ribonuclease H from a three-state folder that populates a kinetic intermediate to one that folds in an apparent two-state fashion. We have compared the folding trajectories of the three-state RNase H and the two-state RNase H, proteins with the same native-state topology but altered regional stability, using a protein engineering approach. Our data suggest that both versions of RNase H fold through a similar trajectory with similar high-energy conformations. Mutations in the core and the periphery of the protein affect similar aspects of folding for both variants, suggesting a common trajectory with folding of the core region followed by the folding of the periphery. Our results suggest that formation of specific partially folded conformations may be a general feature of protein folding that can promote, rather than hinder, efficient folding.
机译：在未折叠状态和天然状态之间的过渡过程中，蛋白质可以采样各种部分折叠的构象。一些蛋白质从不显着地占据这些高能态并通过明显的两态过程折叠。但是，在折叠过程中，许多蛋白质组成了可检测的，部分折叠的形式。这类中间体的作用尚需大量辩论。单个氨基酸变化可以将大肠杆菌核糖核酸酶H从填充动力学中间体的三态文件夹转换为以明显的二态方式折叠的三态文件夹。我们已经使用蛋白质工程方法比较了具有相同原始状态拓扑结构但改变了区域稳定性的三态RNase H和二态RNase H的折叠轨迹。我们的数据表明，两种形式的RNase H均通过具有相似高能构象的相似轨迹折叠。蛋白质核心和外围的突变会影响两个变体折叠的相似方面，这提示了共同的轨迹，核心区域先折叠，然后外围折叠。我们的结果表明，特定的部分折叠构象的形成可能是蛋白质折叠的一般特征，可以促进而不是阻碍有效的折叠。

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