Advillin Folding Takes Place on a Hypersurface of Small Dimensionality
Advillin Folding Takes Place on a Hypersurface of Small Dimensionality
复制标题
DOI：
10.1103/physrevlett.101.208101
复制
发表时间：
2008-11-14
影响因子：
8.6
通讯作者：
Laio, Alessandro
中科院分区：
文献类型：
--
作者：
Piana, Stefano;Laio, Alessandro
全原子显式溶剂分子动力学模拟已被用来调查的拓扑结构的空间探索折叠过程中的C-末端片段的Advillin头，36个氨基酸的蛋白质。分形维数分析表明，在折叠过程中探索的超曲面具有近似的维数只有3。结果表明，这种低维持续远高于展开温度，并不存在于简单的粗粒度模型。
All-atom explicit-solvent molecular dynamics simulations have been used to investigate the topological structure of the space explored during folding by the c-terminal fragment of the Advillin headpiece, a 36 amino-acid protein. A fractal dimension analysis shows that the hypersurface explored during the folding process has an approximate dimensionality of only three. It is shown that this low dimensionality persists well above the unfolding temperature and is not present in simple coarse-grained models.