(2012). Nature Communications, 3(1) , 751. doi: 10.1038/ncomms1738. Article Pubmed
|Protein (state)||t1/2 (s)||Power||Light||Mode||In Cell||Fusion||˚C|
Structural analysis of mTurquoise unveiled one suboptimal residue, Ile146, which was targeted for further improvement... The X-ray structure of the the I146F mutant, dubbed mTurquoise2, reveals that the mutated residue contributes to an improved packing of the chromophore through many further van der Waals interactions. This increases the QY to 0.93, which is now the highest for a monomeric fluorescent protein.