Protein folding transition path times from single molecule FRET.

Protein folding transition path times from single molecule FRET.
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DOI:
10.1016/j.sbi.2017.10.007
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发表时间:
2018-03
影响因子:
6.8
通讯作者:
Eaton WA
Eaton WA
中科院分区:
生物学2区
文献类型:
--
作者:
Chung HS;Eaton WA

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过渡路径是当状态之间的自由能垒被跨越时单个分子轨迹的微小部分,并且对于蛋白质折叠包含了关于自组装机制的所有信息。作为从实验中获得过渡路径期间的结构信息的第一步,单分子FRET光谱已被用于从荧光轨迹的逐光子分析确定平均过渡路径时间。这些结果,获得了几种不同的蛋白质,已经提供了新的和苛刻的测试,支持全原子分子动力学模拟的准确性和蛋白质折叠的能量景观理论的基本假设。
The transition path is the tiny segment of a single molecule trajectory when the free energy barrier between states is crossed and for protein folding contains all of the information about the self-assembly mechanism. As a first step toward obtaining structural information during the transition path from experiments, single molecule FRET spectroscopy has been used to determine average transition path times from a photon-by-photon analysis of fluorescence trajectories. These results, obtained for several different proteins, have already provided new and demanding tests that support both the accuracy of all-atom molecular dynamics simulations and the basic postulates of energy landscape theory of protein folding.
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