Side-chain dynamics and protein folding
Side-chain dynamics and protein folding
复制标题
DOI：
10.1002/prot.10426
复制
发表时间：
2003-08-01
影响因子：
2.9
通讯作者：
Shakhnovich, EI
中科院分区：
文献类型：
--
作者：
Kussell, E;Shimada, J;Shakhnovich, EI
利用晶格模拟和全原子模拟研究了蛋白质侧链在折叠反应中达到平衡的过程。我们发现，侧链松弛的速度在蛋白质结构上呈现出一种分布，松弛最快的侧链位于对折叠具有动力学重要性的位置。主要折叠过渡态的遍历对应于属于折叠核的少量侧链的冻结，而其余的蛋白质通过天然折叠周围的骨架波动走向平衡。侧链松弛的后成核过程具有非常慢的动力学和许多障碍穿越的特点，因此类似于玻璃的行为。(C)2003年Wiley-Liss，Inc.
The processes by which protein side chains reach equilibrium during a folding reaction are investigated using both lattice and all-atom simulations. We find that rates of side-chain relaxation exhibit a distribution over the protein structure, with the fastest relaxing side chains located in positions kinetically important for folding. Traversal of the major folding transition state corresponds to the freezing of a small number of side chains, belonging to the folding nucleus, whereas the rest of the protein proceeds toward equilibrium via backbone fluctuations around the native fold. The postnucleation processes by which side chains relax are characterized by very slow dynamics and many barrier crossings, and thus resemble the behavior of a glass. (C) 2003 Wiley-Liss, Inc.