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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Folding and misfolding of the papillomavirus E6 interacting peptide E6ap
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Folding and misfolding of the papillomavirus E6 interacting peptide E6ap

机译：乳头瘤病毒E6相互作用肽E6ap的折叠和错误折叠

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All-atom Langevin dynamics simulations have been performed to study the folding pathways of the 18-residue binding domain fragment E6ap of the human papillomavirus E6 interacting peptide. Six independent folding trajectories, with a total duration of nearly 2 mus, all lead to the same native state in which the E6ap adopts a fluctuating a-helix structure in the central portion (Ser-4-Leu-13) but with very flexible N and C termini. Simulations starting from different core configurations exhibit the E6ap folding dynamics as either a two- or three-state folder with an intermediate misfolded state. The essential leucine hydrophobic core (Leu-9, Leu-12, and Leu-13) is well conserved in the native-state structure but absent in the intermediate structure, suggesting that the leucine core is not only essential for the binding activity of E6ap but also important for the stability of the native structure. The free energy landscape reveals a significant barrier between the basins separating the native and misfolded states. We also discuss the various underlying forces that drive the peptide into its native state. [References: 48]
机译：已经进行了全原子朗格文动力学模拟，以研究人乳头瘤病毒E6相互作用肽的18个残基结合域片段E6ap的折叠途径。六个独立的折叠轨迹（总持续时间将近2 mus）都导致相同的原始状态，其中E6ap在中央部分（Ser-4-Leu-13）采用波动的a螺旋结构，但N和C总站。从不同核心配置开始的仿真显示E6ap折叠动力学为处于中间错误折叠状态的两状态或三状态折叠器。必需的亮氨酸疏水核心（Leu-9，Leu-12和Leu-13）在原始状态结构中非常保守，但在中间结构中却不存在，这表明亮氨酸核心不仅对于E6ap的结合活性至关重要而且对于本地结构的稳定性也很重要。自由能的格局揭示了在将原始状态和错误折叠状态分开的盆地之间的重大障碍。我们还讨论了驱动肽进入其天然状态的各种潜在作用力。 [参考：48]

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