A genetically encoded infrared probe.

Kathryn C Schultz, Lubica Supekova, Youngha Ryu, Jianming Xie, Roshan Perera, Peter G Schultz

Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. schultz@scripps.edu

Journal of the American Chemical Society 2006 Nov 1

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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.

Citation

Kathryn C Schultz, Lubica Supekova, Youngha Ryu, Jianming Xie, Roshan Perera, Peter G Schultz. A genetically encoded infrared probe. Journal of the American Chemical Society. 2006 Nov 1;128(43):13984-5