Faculty Profiles - MURAKAMI Hiroshi

Papers - MURAKAMI Hiroshi

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A non-natural amino acid for efficient incorporation into proteins as a sensitive fluorescent probe

Taki, M. and Hohsaka, T. and Murakami, H. and Taira, K. and Sisido, M.

FEBS Letters Vol. 507 ( 1 ) page： 35-38 2001

Five-base codons for incorporation of nonnatural amino acids into proteins Open Access

Hohsaka, T. and Ashizuka, Y. and Murakami, H. and Sisido, M.

Nucleic Acids Res. Vol. 29 ( 17 ) page： 3646-3651 2001

Incorporation of nonnatural amino acids into proteins by using various four-base codons in an Escherichia coli in vitro translation system

Hohsaka, T. and Ashizuka, Y. and Taira, H. and Murakami, H. and Sisido, M.

Biochemistry Vol. 40 ( 37 ) page： 11060-11064 2001

Five-base codons for incorporation of nonnatural amino acids into proteins Open Access

Hohsaka, T, Ashizuka, Y, Murakami, H, Sisido, M

Nucleic Acids Res. Vol. 29 ( 17 ) page： 3646-3651 2001

Site-Directed Incorporation of Fluorescent Nonnatural Amino Acids into Streptavidin for Highly Sensitive Detection of Biotin

Hiroshi Murakami, Takahiro Hohsaka, Yuki Ashizuka, Kimiko Hashimoto, Masahiko Sisido

Biomacromolecules Vol. 1 ( 1 ) page： 118 - 125 2000.3

Language：English Publishing type：Research paper (scientific journal) Publisher：American Chemical Society ({ACS})

Fluorescent nonnatural amino acids were incorporated into specific positions of streptavidin. The positions of the nonnatural amino acids were directed by a CGGG/CCCG four-base codon/anticodon pair. The nonnatural mutants with a single 2-anthrylalanine at the 22nd, 43rd, 54th, and 120th positions, respectively, were found to bind biotin, indicating that the mutants retained active conformation. The fluorescence intensities of the anthryl groups were relatively insensitive to the positions and the biotin binding when excited at 265 nm. When the anthryl group at the 120th position was excited through energy transfer from tryptophan units, the fluorescence intensity markedly decreased with biotin binding, because of a suppression of the energy transfer. Amino acids carrying 7-methoxycoumarine fluorophore were also incorporated at the 120th position Their fluorescence quantum yields were very sensitive to the biotin binding. The high sensitivity of the coumarine-labeled streptavidin exemplifies potential applications of fluorescent nonnatural mutants for detecting specific molecules at very low concentrations.

DOI： 10.1021/bm990012g

Scopus

PubMed

A chiral Eu3+-thienoyltrifluoroacetone complex on an avidin tetramer: luminescence and CD studies on the supramolecular protein-metal chelate complex

Taki, M. and Murakami, H. and Sisido, M.

Chem. Commun. ( 13 ) page： 1199-1200 2000

A chiral Eu3+–thienoyltrifluoroacetone complex on an avidin tetramer: luminescence and CD studies on the supramolecular protein–metal chelate complex

Masumi Taki, Hiroshi Murakami, Masahiko Sisido

Chemical Communications ( 13 ) page： 1199 - 1200 2000

Efficient incorporation of nonnatural amino acids with large aromatic groups into streptavidin in in vitro protein synthesizing systems

Hohsaka, T. and Kajihara, D. and Ashizuka, Y. and Murakami, H. and Sisido, M.

J. Am. Chem. Soc. Vol. 121 ( 1 ) page： 34-40 1999

Incorporation of two different nonnatural amino acids independently into a single protein through extension of the genetic code

Hohsaka, T. and Ashizuka, Y. and Sasaki, H. and Murakami, H. and Sisido, M.

J. Am. Chem. Soc. Vol. 121 ( 51 ) page： 12194-12195 1999

Site-directed incorporation of p-nitrophenylalanine into streptavidin and site-to-site photoinduced electron transfer from a pyrenyl group to a nitrophenyl group on the protein framework

Murakami, H. and Hohsaka, T. and Ashizuka, Y. and Sisido, M.

J. Am. Chem. Soc. Vol. 120 ( 30 ) page： 7520-7529 1998

Incorporation of nonnatural amino acids into streptavidin through in vitro frame-shift suppression

Hohsaka, T. and Ashizuka, Y. and Murakami, H. and Sisido, M.

J. Am. Chem. Soc. Vol. 118 ( 40 ) page： 9778-9779 1996

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Papers - MURAKAMI Hiroshi