The Genetic Incorporation of a Distance Probe into Proteins in Escherichia coli | Zendy

MengLin Tsao | Zendy; Daniel Summerer | Zendy; Youngha Ryu | Zendy; Peter G. Schultz | Zendy

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The Genetic Incorporation of a Distance Probe into Proteins in Escherichia coli

Author(s) -

MengLin Tsao,

Daniel Summerer,

Youngha Ryu,

Peter G. Schultz

Publication year - 2006

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/ja058262u

Subject(s) - chemistry , escherichia coli , transfer rna , leucine zipper , genetic code , zipper , amino acid , aminoacyl trna synthetase , nonsense mutation , biochemistry , function (biology) , fluorescence , biophysics , mutation , genetics , rna , peptide sequence , gene , biology , physics , algorithm , quantum mechanics , missense mutation , computer science

The unnatural amino acid p-nitrophenylalanine (pNO2-Phe) was genetically introduced into proteins in Escherichia coli in response to the amber nonsense codon with high fidelity and efficiency by means of an evolved tRNA/aminoacyl-tRNA synthetase pair from Methanocuccus jannaschii. It was shown that pNO2-Phe efficiently quenches the intrinsic fluorescence of Trp in a distance-dependent manner in a model GCN4 basic region leucine zipper (bZIP) protein. Thus, the pNO2-Phe/Trp pair should be a useful biophysical probe of protein structure and function.

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