All-atom structure prediction and folding simulations of a stable protein
All-atom structure prediction and folding simulations of a stable protein
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DOI：
10.1021/ja0273851
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发表时间：
2002-09-25
影响因子：
15
通讯作者：
Roitberg, AE
中科院分区：
文献类型：
--
作者：
Simmerling, C;Strockbine, B;Roitberg, AE
我们展示了一个具有非平凡二级结构元素和疏水核心的稳定蛋白质的全原子、完全不受约束的从头计算折叠模拟结果。这种名为“trpcage”的结构是由华盛顿大学安德森小组优化的20个残基序列，是目前显示两态折叠特性的最小蛋白质。与实验结构的明确区域相比，我们的预测具有非常低的0.97 Å c α均方根偏差（rmsd）和1.4 Å。模拟结构族显示了实验数据所建议的附加特征，但在核磁共振衍生结构族中并不明显。
We present results from all-atom, fully unrestrained ab initio folding simulations for a stable protein with nontrivial secondary structure elements and a hydrophobic core. The construct, “trpcage”, is a 20-residue sequence optimized by the Andersen group at University of Washington and is currently the smallest protein that displays two-state folding properties. Compared over the well-defined regions of the experimental structure, our prediction has a remarkably low 0.97 Å Cαroot-mean-square-deviation (rmsd) and 1.4 Å for all heavy atoms. The simulated structure family displays additional features that are suggested by experimental data, yet are not evident in the family of NMR-derived structures.