In VitroSite-Specific Incorporation of Fluorescent Probes into β-Galactosidase

Autor:	J. B. Alexander Ross,‡ and, A. Richard Chamberlin, Justin E. Carlson, Lance E. Steward, Marcella A. Gilmore, Cynthia S. Collins
Rok vydání:	1997
Předmět:	chemistry.chemical_classification Tryptophan Chemical modification General Chemistry Biochemistry Fluorescence Catalysis In vitro Fluorescence spectroscopy Amino acid Colloid and Surface Chemistry Protein structure chemistry Function (biology)
Zdroj:	Journal of the American Chemical Society. 119:6-11
ISSN:	1520-5126 0002-7863
DOI:	10.1021/ja963023f
Popis:	Fluorescence spectroscopy is a powerful biophysical technique for studying protein structure, function, dynamics, and intermolecular interactions. Such studies are often conducted using intrinsic probes, such as tryptophan residues, or extrinsic probes introduced by post-translational modification, such as dansyl. Specificity, however, is often a concern since many proteins contain more than one tryptophan and chemical modification often will occur at more than one site. Herein we report the in vitro, site-specific incorporation of three fluorescent amino acid analogues, 5-hydroxytryptophan, 7-azatryptophan, and e-dansyllysine, each of which was incorporated into β-galactosidase at a single designated site.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::dbefd8d27b3628131a759c6d6d6b39c0 https://doi.org/10.1021/ja963023f Zobrazit plný text záznamu