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  • Title: Position-specific incorporation of biotinylated non-natural amino acids into a protein in a cell-free translation system.
    Author: Watanabe T, Muranaka N, Iijima I, Hohsaka T.
    Journal: Biochem Biophys Res Commun; 2007 Sep 28; 361(3):794-9. PubMed ID: 17678619.
    Abstract:
    Biotinylation is useful for the detection, purification and immobilization of proteins. It is performed by chemical modification, although position-specific and quantitative biotinylation is rarely achieved. We developed a position-specific biotinylation method using biotinylated non-natural amino acids. We showed that biotinylated p-aminophenylalanine derivatives were incorporated into a protein more efficiently than biotinylated lysine derivatives in a cell-free translation system. In addition, the biotinylated p-aminophenylalanines overcame the serious position-dependency observed for biotinylated lysines. The present method will be useful for detection and purification of proteins along with comprehensive exploration of surface-exposed residues and oriented immobilization of proteins.
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