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Inside Cover: Effects of FlAsH/Tetracysteine (TC) Tag on PrP Proteolysis and PrPres Formation by TC‐Scanning (ChemBioChem 13/2013)
Author(s) -
Taguchi Yuzuru,
Hohsfield Lindsay A.,
Hollister Jason R.,
Baron Gerald S.
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.201390047
Subject(s) - proteolysis , trypsin , flash (photography) , cover (algebra) , chemistry , cleavage (geology) , graphics , microbiology and biotechnology , fluorescence , stereochemistry , biophysics , biochemistry , computer graphics (images) , biology , computer science , physics , optics , enzyme , engineering , mechanical engineering , fracture (geology) , paleontology
The inside cover picture shows a mapping technique by Y. Taguchi, L. A. Hohsfield, G. S. Baron et al. (see p. 1597 ff. ). Tetracysteine (TC) motifs bind fluorescent biarsenical dyes (FlAsH). Positions where FlAsH/TC insertion into PrP inhibits trypsin cleavage are detected by SDS‐PAGE, thus localizing points of contact between PrP and trypsin. Thanks to Darrell Hurt (BCBB, NIAID) and Austin Athman for graphics assistance.