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

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• 作者：Meng-Lin Tsao ; Daniel Summerer ; Youngha Ryu ; and Peter G. Schultz
• 刊名：Journal of the American Chemical Society
• 出版年：2006
• 出版时间：April 12, 2006
• 年：2006
• 卷：128
• 期：14
• 页码：4572 - 4573
• 全文大小：122K
• 年卷期：v.128,no.14(April 12, 2006)
• ISSN：1520-5126

文摘

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.