Force-dependent mechanical unfolding pathways of GFP
Force-dependent mechanical unfolding pathways of GFP
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DOI：
10.1016/j.eml.2015.12.001
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发表时间：
2016-09-01
影响因子：
4.7
通讯作者：
Park, Harold S.
中科院分区：
文献类型：
--
作者：
Cao, Penghui;Tao, Weiwei;Park, Harold S.
我们使用基于势能面探索的新型原子模拟来表征绿色荧光蛋白(GFP)依赖于力的展开路径和中间构型。通过使用这种方法，与以前的原子模拟研究相比，我们能够将GFP展开到显著更长的端到端距离，即40 nm。我们发现在5到40 nm之间存在四个中间态，其中中间构型和展开路径强烈依赖于力。此外，我们还计算了14 nmα-β(1)中间体的力相关寿命，并证明了它服从贝尔公式。(C)2015爱思唯尔有限公司。保留所有权利。
Wecharacterize the force-dependent unfolding pathways and intermediate configurations of the green fluorescence protein (GFP) using novel atomistic simulations based on potential energy surface exploration. By using this approach, we are able to unfold GFP to significantly longer end-to-end distances, i.e. 40 nm, as compared to that seen in previous atomistic simulation studies. We find that there are four intermediate states between 5 and 40 nm end-to-end distance, where the intermediate configurations and unfolding pathways are strongly force-dependent. We additionally calculate the force-dependent lifetime of the 14 nm alpha beta(1) intermediate, and demonstrate that it obeys Bell's formula. (C) 2015 Elsevier Ltd. All rights reserved.