title: A genetically encoded infrared probe.
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.
authors.affiliation: 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
authors.forename: Kathryn C
authors.initials: KC
authors.lastname: Schultz
authors.forename: Lubica
authors.initials: L
authors.lastname: Supekova
authors.forename: Youngha
authors.initials: Y
authors.lastname: Ryu
authors.forename: Jianming
authors.initials: J
authors.lastname: Xie
authors.forename: Roshan
authors.initials: R
authors.lastname: Perera
authors.forename: Peter G
authors.initials: PG
authors.lastname: Schultz
mesh_terms: D008958:Models, Molecular; D015335:Molecular Probes; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D015335:Molecular Probes