The crystal structure of red fluorescent protein TagRFP-T reveals the mechanism of its superior photostability
The crystal structure of red fluorescent protein TagRFP-T reveals the mechanism of its superior photostability
复制标题
红色荧光蛋白TagRFP-T的晶体结构揭示了其优越光稳定性的机制
DOI：
10.1016/j.bbrc.2016.06.047
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发表时间：
2016-08-19
影响因子：
3.1
通讯作者：
Ding, Yu
中科院分区：
文献类型：
--
作者：
Liu, Rui;Liang, Qing-Nan;Ding, Yu
The red fluorescent protein variant TagRFP-T has greatly improved photostability over its parent molecule, TagRFP, but the underlying mechanism leading to this improvement is to date unknown. The 1.95 angstrom resolution crystallographic structure of TagRFP-T showed that its chromophore exists as a mixture of cis and trans coplanar isomers in roughly equal proportions. Interestingly, both isomers are able to fluoresce, a property that has never been observed in any other fluorescent protein. We propose a "circular restoration model" for TagRFP-T to explain its superior photostability: There are four co-existing chromophore states (cis/trans protonatediionized state) that can be driven by light to transform from one state into another. This model also explains how TagRPF-T essentially eliminates the temporary dark state (reversible photobleaching). (C) 2016 Elsevier Inc. All rights reserved.
