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Inside Cover: Protein Arginine Allylation and Subsequent Fluorophore Targeting (ChemBioChem 12/2013)
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 - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201390043
Subject(s) - fluorophore , chemistry , tetrazole , alkylation , protein methylation , cover (algebra) , stereochemistry , methyltransferase , combinatorial chemistry , methylation , fluorescence , biochemistry , dna , mechanical engineering , physics , quantum mechanics , engineering , catalysis
The inside cover picture shows protein methyltransferase‐mediated alkylation in the presence of S ‐adenosyl‐ L ‐methionine (SAM) and its allylated analogue. On p. 1438 ff. , Z. K. Zhao et al. relate how they discovered that allyl‐SAM acts as an excellent SAM surrogate leading to protein allylation, and that the allyl group enables subsequent fluorophore targeting upon reaction with tetrazole compounds.