将距离探针基因掺入大肠杆菌中的蛋白质。
The genetic incorporation of a distance probe into proteins in Escherichia coli.
作者信息
Tsao Meng-Lin, Summerer Daniel, Ryu Youngha, Schultz Peter G
机构信息
Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
出版信息
J Am Chem Soc. 2006 Apr 12;128(14):4572-3. doi: 10.1021/ja058262u.
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.
通过来自詹氏甲烷球菌（Methanocuccus jannaschii）进化而来的tRNA/氨酰tRNA合成酶对，非天然氨基酸对硝基苯丙氨酸（pNO2-Phe）以高保真度和效率在大肠杆菌中通过琥珀色无义密码子被遗传引入蛋白质中。结果表明，在模型GCN4碱性区域亮氨酸拉链（bZIP）蛋白中，pNO2-Phe以距离依赖的方式有效地淬灭了色氨酸的固有荧光。因此，pNO2-Phe/色氨酸对应该是一种用于蛋白质结构和功能研究的有用生物物理探针。
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