A polarizable embedding DFT study of one-photon absorption in fluorescent proteins
A polarizable embedding DFT study of one-photon absorption in fluorescent proteins
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DOI：
10.1039/c3cp44659j
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发表时间：
2013-01-01
影响因子：
3.3
通讯作者：
Olsen, Jogvan Magnus Haugaard
中科院分区：
文献类型：
--
作者：
Beerepoot, Maarten T. P.;Steindal, Arnfinn Hykkerud;Olsen, Jogvan Magnus Haugaard
对五种荧光蛋白(FP)的单光子吸收进行了理论研究。用极化包埋法结合密度泛函理论(PE-DFT)计算了野生型绿色荧光蛋白(WtGFP)及其突变体(BFP、EGFP、YFP和eCFP)的吸收性质。当直接对晶体结构进行计算或使用从分子动力学模拟中提取的结构时，我们的方法重现了观察到的FP之间的激发能趋势。然而，在前一种情况下，为了重现实验趋势，需要在冷冻蛋白质环境中对生色团进行QM/MM几何优化。要在不同的FP之间产生正确的趋势，不需要对力场中的极化进行明确的解释，但这对于重现实验观察到的从真空到蛋白质的红移是必要的。这是使用可极化嵌入电势对一系列荧光蛋白质进行的第一次计算研究。
A theoretical study of the one-photon absorption of five fluorescent proteins (FPs) is presented. The absorption properties are calculated using a polarizable embedding approach combined with density functional theory (PE-DFT) on the wild-type green fluorescent protein (wtGFP) and several of its mutants (BFP, eGFP, YFP and eCFP). The observed trends in excitation energies among the FPs are reproduced by our approach when performing calculations directly on the crystal structures or when using structures extracted from molecular dynamics simulations. However, in the former case, QM/MM geometry optimization of the chromophores within a frozen protein environment is needed in order to reproduce the experimental trends. An explicit account of polarization in the force field is not needed to yield the correct trend between the different FPs, but it is necessary for reproducing the experimentally observed red shift from vacuum to protein. This is the first computational study of a range of fluorescent proteins using a polarizable embedding potential.