A novel fluorescent nonnatural amino acid that can be incorporated into a specific position of streptavidin
Author(s) -
Masumi Taki,
Takahiro Hohsaka,
Hitoshi Murakami,
Atsushi Kuno,
Tatsuya Hasegawa,
Kazunari Taira,
Masahiko Sisido
Publication year - 2002
Publication title -
nucleic acids symposium series
Language(s) - English
Resource type - Journals
eISSN - 1746-8272
pISSN - 0261-3166
DOI - 10.1093/nass/2.1.203
Subject(s) - streptavidin , fluorescence , biotin , amino acid , beta (programming language) , biotinylation , chemistry , mutant , transfer rna , alpha (finance) , stereochemistry , biochemistry , rna , physics , computer science , mathematics , construct validity , statistics , quantum mechanics , gene , programming language , psychometrics
A novel highly fluorescent nonnatural amino acid (beta-(N-methylanthraniloyl)-L-alpha,beta-diaminopropionic acid; nmaDap) was incorporated at the 120th position of streptavidin. The position was directed by a CGGG/CCCG four-base codon/anticodon pair. The incorporation efficiency and the biotin-binding ability of the nmaDap mutant were compared to those of beta-anthraniloyl-L-alpha,beta-diaminopropionic acid (atnDap).
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