| Literature DB >> 17061854 |
Kathryn C Schultz1, Lubica Supekova, Youngha Ryu, Jianming Xie, Roshan Perera, Peter G Schultz.
Abstract
An orthogonal tRNA/aminoacyl-tRNA synthetase pair has been evolved that makes it possible to selectively and efficiently incorporate para-cyanophenylalanine (pCNPhe) into proteins in E. coli at sites specified by the amber nonsense codon, TAG. Substitution of pCNPhe for histidine-64 in myoglobin (Mb) affords a sensitive vibrational probe of ligand binding. This methodology provides a useful infrared reporter of protein structure, biomolecular interactions, and conformational changes.Entities:
Mesh：
Substances：
Year: 2006 PMID： 17061854 DOI： 10.1021/ja0636690
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419