Site-specific labeling of proteins with NMR-active unnatural amino acids

被引：0
作者：
David H. Jones
Susan E. Cellitti
Xueshi Hao
Qiong Zhang
Michael Jahnz
Daniel Summerer
Peter G. Schultz
Tetsuo Uno
Bernhard H. Geierstanger
机构：
[1] Genomics Institute of the Novartis Research Foundation,Department of Chemistry and the Skaggs Institute for Chemical Biology
[2] The Scripps Research Institute,undefined
来源：
Journal of Biomolecular NMR | 2010年 / 46卷
关键词：
Site-specific labeling; Unnatural amino acids; Spin label; Metal chelator; In-cell NMR;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
A large number of amino acids other than the canonical amino acids can now be easily incorporated in vivo into proteins at genetically encoded positions. The technology requires an orthogonal tRNA/aminoacyl-tRNA synthetase pair specific for the unnatural amino acid that is added to the media while a TAG amber or frame shift codon specifies the incorporation site in the protein to be studied. These unnatural amino acids can be isotopically labeled and provide unique opportunities for site-specific labeling of proteins for NMR studies. In this perspective, we discuss these opportunities including new photocaged unnatural amino acids, outline usage of metal chelating and spin-labeled unnatural amino acids and expand the approach to in-cell NMR experiments.
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页码：89 / 100
页数：11
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