title: Simple and inexpensive incorporation of 19F-tryptophan for protein NMR spectroscopy.
abstract: Fluorine-containing amino acids are valuable probes for the biophysical characterization of proteins. Current methods for (19)F-labeled protein production involve time-consuming genetic manipulation, compromised expression systems and expensive reagents. We show that Escherichia coli BL21, the workhorse of protein production, can utilise fluoroindole for the biosynthesis of proteins containing (19)F-tryptophan.
authors.affiliation: School of Chemistry, National University of Ireland Galway, University Road, Galway, Ireland. peter.crowley@nuigalway.ie
authors.forename: Peter B
authors.initials: PB
authors.lastname: Crowley
authors.forename: Ciara
authors.initials: C
authors.lastname: Kyne
authors.forename: William B
authors.initials: WB
authors.lastname: Monteith
mesh_terms: D004926:Escherichia coli / Q000378:metabolism; D005461:Fluorine / Q000737:chemistry; D007211:Indoles / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D014364:Tryptophan / Q000737:chemistry*
chemical_list: D007211:Indoles; D011506:Proteins; D005461:Fluorine; C095066:5-fluoroindole; D014364:Tryptophan