Comparison of monomeric variants of StayGold
Miyawaki, A.; Shimozono, S.; Ando, R.; Sugiyama, M.; Hirano, M.; Niino, Y.
Show abstract
StayGold is a bright and highly photostable fluorescent protein (FP) that forms an obligate dimer, thereby limiting its application as a soluble marker. On the basis of the structural information of this FP, we disrupted the dimerization to generate a monomeric variant, mStayGold, which inherits both the extremely high photostability and the high practical brightness of StayGold, for molecular fusion and membrane-targeting applications. Meanwhile, two other research groups have independently monomerized StayGold using different strategies. As a result, multiple StayGold monomers are currently available, creating confusion in the research community. In the present study, we investigated the three basic properties--photostability, brightness, and dispersibility--of these monomers by performing detailed side-by-side comparisons. This study highlights the difficulties of StayGold monomerization with emphasis on the tradeoff between photostability and brightness in FP technology.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
Similar papers in this journal
- A fluorogenic chemically induced dimerization technology for controlling, imaging and sensing protein proximity 95%
- Engineered allostery in light-regulated LOV-Turbo enables precise spatiotemporal control of proximity labeling in living cells 94%
- HaloTag9: an engineered protein tag to improve fluorophore performance 94%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.