The role of cysteine residues in the allosteric modulation of the chromophore phototransformations of biphotochromic fluorescent protein SAASoti
Abstract Biphotochromic fluorescent protein SAASoti contains five cysteine residues in its sequence and a V127T point mutation transforms it to the monomeric form, mSAASoti. These cysteine residues are located far from the chromophore and might control its properties only allosterically. The influen...
Main Authors: | A. V. Gavshina, N. K. Marynich, M. G. Khrenova, I. D. Solovyev, A. P. Savitsky |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2021-12-01
|
Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-021-03634-9 |
Similar Items
-
First biphotochromic fluorescent protein moxSAASoti stabilized for oxidizing environment
by: N. K. Marynich, et al.
Published: (2022-05-01) -
The Role of the 145 Residue in Photochemical Properties of the Biphotochromic Protein mSAASoti: Brightness versus Photoconversion
by: Alexandra V. Gavshina, et al.
Published: (2022-12-01) -
The role of the correlated motion(s) of the chromophore in photoswitching of green and red forms of the photoconvertible fluorescent protein mSAASoti
by: Alexandra V. Gavshina, et al.
Published: (2024-04-01) -
Reversible photobleaching of photoconvertible SAASoti-FP
by: Ilya D. Solovyev, et al.
Published: (2017-12-01) -
Monomerization of the photoconvertible fluorescent protein SAASoti by rational mutagenesis of single amino acids
by: Ilya D. Solovyev, et al.
Published: (2018-10-01)