z-logo
open-access-imgOpen Access
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).

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom