anticodon and 4-nitrophenylalanine

anticodon has been researched along with 4-nitrophenylalanine* in 2 studies

Other Studies

2 other study(ies) available for anticodon and 4-nitrophenylalanine

Article	Year
Efficient incorporation of a nonnatural amino acid into a protein in an insect cell-free translation system. Nucleic acids symposium series (2004), 2006, Issue:50 Recently, we have succeeded in incorporating various nonnatural amino acids into proteins by using four-base codon-anticodon pairs in Spodoptera frugiperda 21 (Sf21) insect cell-free protein synthesizing system. Here, the reaction was conducted under various conditions in order to optimize the incorporation efficiency. The optimal concentration of aminoacyl-tRNA, reaction temperature, and reaction time were 2 nM, 25 degrees C, and 1.5 hr, respectively. Topics: Amino Acids; Animals; Anticodon; Cell-Free System; Phenylalanine; Protein Biosynthesis; Protein Engineering; RNA, Transfer, Amino Acyl; Spodoptera; Streptavidin; Temperature	2006
Position-specific incorporation of a fluorophore-quencher pair into a single streptavidin through orthogonal four-base codon/anticodon pairs. Journal of the American Chemical Society, 2002, Dec-11, Volume: 124, Issue:49 Four-base codon strategy was applied to incorporate a fluorophore-quencher pair into specific positions on a single protein; beta-anthraniloyl-L-alpha,beta-diaminopropionic acid (atnDap) was employed as a fluorophore and p-nitrophenylalanine (ntrPhe) as a quencher. Their positions were directed by the CGGG/CCCG and GGGC/CCCG four-base codon/anticodon pairs and two doubly mutated streptavidins, i.e., ((52)atnDap, (84)ntrPhe) and ((54)ntrPhe, (84)atnDap) mutants were synthesized through Escherichia coli in vitro protein synthesizing systems. Intramolecular photoinduced electron transfer (ET) was observed as the decrease of intensity in steady-state fluorescence spectroscopy and as the shortening of fluorescence decaytimes. The quenching data indicated that the ET rate reflects the detailed structure of the protein. Topics: Amino Acids; Anticodon; Biotin; Codon; Computer Simulation; Electrons; Escherichia coli; Fluorescent Dyes; Models, Molecular; ortho-Aminobenzoates; Phenylalanine; Protein Conformation; Protein Engineering; Spectrometry, Fluorescence; Streptavidin	2002

Article

Year

Efficient incorporation of a nonnatural amino acid into a protein in an insect cell-free translation system.

Nucleic acids symposium series (2004), 2006, Issue:50

Recently, we have succeeded in incorporating various nonnatural amino acids into proteins by using four-base codon-anticodon pairs in Spodoptera frugiperda 21 (Sf21) insect cell-free protein synthesizing system. Here, the reaction was conducted under various conditions in order to optimize the incorporation efficiency. The optimal concentration of aminoacyl-tRNA, reaction temperature, and reaction time were 2 nM, 25 degrees C, and 1.5 hr, respectively.

Topics: Amino Acids; Animals; Anticodon; Cell-Free System; Phenylalanine; Protein Biosynthesis; Protein Engineering; RNA, Transfer, Amino Acyl; Spodoptera; Streptavidin; Temperature

2006

Position-specific incorporation of a fluorophore-quencher pair into a single streptavidin through orthogonal four-base codon/anticodon pairs.

Journal of the American Chemical Society, 2002, Dec-11, Volume: 124, Issue:49

Four-base codon strategy was applied to incorporate a fluorophore-quencher pair into specific positions on a single protein; beta-anthraniloyl-L-alpha,beta-diaminopropionic acid (atnDap) was employed as a fluorophore and p-nitrophenylalanine (ntrPhe) as a quencher. Their positions were directed by the CGGG/CCCG and GGGC/CCCG four-base codon/anticodon pairs and two doubly mutated streptavidins, i.e., ((52)atnDap, (84)ntrPhe) and ((54)ntrPhe, (84)atnDap) mutants were synthesized through Escherichia coli in vitro protein synthesizing systems. Intramolecular photoinduced electron transfer (ET) was observed as the decrease of intensity in steady-state fluorescence spectroscopy and as the shortening of fluorescence decaytimes. The quenching data indicated that the ET rate reflects the detailed structure of the protein.

Topics: Amino Acids; Anticodon; Biotin; Codon; Computer Simulation; Electrons; Escherichia coli; Fluorescent Dyes; Models, Molecular; ortho-Aminobenzoates; Phenylalanine; Protein Conformation; Protein Engineering; Spectrometry, Fluorescence; Streptavidin

2002