Structural highlights
Publication Abstract from PubMed
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 A 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 protonated/ionized 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).
The crystal structure of red fluorescent protein TagRFP-T reveals the mechanism of its superior photostability.,Liu R, Liang QN, Du SQ, Hu XJ, Ding Y Biochem Biophys Res Commun. 2016 Aug 19;477(2):229-34. doi:, 10.1016/j.bbrc.2016.06.047. Epub 2016 Jun 11. PMID:27297107[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu R, Liang QN, Du SQ, Hu XJ, Ding Y. The crystal structure of red fluorescent protein TagRFP-T reveals the mechanism of its superior photostability. Biochem Biophys Res Commun. 2016 Aug 19;477(2):229-34. doi:, 10.1016/j.bbrc.2016.06.047. Epub 2016 Jun 11. PMID:27297107 doi:http://dx.doi.org/10.1016/j.bbrc.2016.06.047
