No spectrum has been submitted ... but a protein must have at least one state first. Add a state.
Oligomerization | Organism | Molecular Weight | Cofactor |
---|---|---|---|
Monomer | Aequorea victoria | 26.9 kDa | - |
This protein does not yet have any fluorescent states assigned. Submit a change.
No photostability measurements available ... add one!
mTurquoise2-G was derived from mTurquoise2 with the following mutations: D148G
amino acid numbers relative to avGFP. show relative to mTurquoise2
To test whether a glycine instead of the aspartate at position 148 could be beneficial for mTurquoise2, we introduced this mutation and crystalized this protein along with the mTurquoise-D148G variant (Von Stetten et al., PDB entry 4B5Y). It was found that in mTurquoise the D148G mutation cased increased van der Waals contact with the isoleucine at position 146. Introducing the D148G mutation into mTurquoise2 with a phenylalanine at position 146 demonstrated that no further stabilization of the contacts between the chromophore and Phe146 could be achieved. Instead, this study revealed that the more flexible beta-strand 7, with the glycine at position 146, now introduced a slightly higher susceptibility towards photobleaching in mTurquoise2-G as compared to mTurquoise2. Source: https://books.google.com.au/books?id=CYKbBgAAQBAJ&printsec=frontcover#v=onepage&q=D148G&f=false
von Stetten et al. (2013)
(2013). , , . doi: 10.2210/pdb4b5y/pdb. Article
Something missing or incorrect? Submit a change Submit a change