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Protein Arginine Allylation and Subsequent Fluorophore Targeting
Author(s) -
Zhang Yixin,
Pan Yanbo,
Yang Wei,
Liu Wujun,
Zou Hanfa,
Zhao Zongbao K.
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201300176
Subject(s) - fluorophore , tetrazole , chemistry , arginine , yeast , fluorescence , ribonucleoprotein , combinatorial chemistry , biochemistry , stereochemistry , amino acid , rna , physics , quantum mechanics , gene
Protein allylation and fluorophore targeting: Arginine residues of the yeast nuclear ribonucleoprotein Npl3 were extensively modified by Hmt1‐catalyzed allylation reaction with allyl‐SAM as the allyl group donor. The allylated protein was further treated with tetrazole compounds under UV irradiation, leading to formation of protein‐attached fluorescent products.