How native-state topology affects the folding of dihydrofolate reductase and interleukin-1β
How native-state topology affects the folding of dihydrofolate reductase and interleukin-1β
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DOI：
10.1073/pnas.100547897
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发表时间：
2000-05-23
影响因子：
11.1
通讯作者：
Onuchic, JN
中科院分区：
文献类型：
--
作者：
Clementi, C;Jennings, PA;Onuchic, JN
实验观察到的二氢叶酸还原酶和白细胞介素-1β的过渡态和中间体整体的整体结构可以通过使用几乎没有能量挫败的简化模型来获得。这些模型的预测能力表明，即使对于这些具有完全不同折叠机制和功能的非常大的蛋白质，真实的蛋白质序列也经过充分设计，并且在结构中观察到的大部分结构异质性。 中间体和过渡态系综是由拓扑效应决定的。
The overall structure of the transition-state and intermediate ensembles observed experimentally for dihydrofolate reductase and interleukin-1 beta can be obtained by using simplified models that have almost no energetic frustration, The predictive power of these models suggests that, even for these very large proteins with completely different folding mechanisms and functions, real protein sequences are sufficiently well designed, and much of the structural heterogeneity observed in the intermediates and the transition-state ensembles is determined by topological effects.