The structure of the dimeric form of rsCherryRev1.4 shows an unusual disulfide-linked dimerization that might be useful in the development of redox-sensitive biosensors in oxidizing environments
#DisulfideBonds #Oligomerization #FluorescentProteins https://doi.org/10.1107/S2053230X23000572
An unusual disulfide-linked dimerization in the fluorescent protein rsCherryRev1.4
The 2 Å resolution crystal structure of rsCherryRev1.4 illustrates dimer formation via a disulfide linkage in a fluorescent protein.
Thi Yen Hang Bui et al.: An unusual disulfide-linked dimerization in the fluorescent protein rsCherryRev1.4
#DisulfideBonds #Oligomerization #FluorescentProteins ...
#IUCr http://scripts.iucr.org/cgi-bin/paper?S2053230X23000572An unusual disulfide-linked dimerization in the fluorescent protein rsCherryRev1.4
The 2 Å resolution crystal structure of rsCherryRev1.4 illustrates dimer formation via a disulfide linkage in a fluorescent protein.
StructBiolCommunications