Premium
A Cost‐Effective Labeling Strategy for the NMR Study of Large Proteins: Selective 15 N‐Labeling of the Tryptophan Side Chains of Prolyl Oligopeptidase
Author(s) -
Tarragó Teresa,
Claasen Birgit,
Kichik Nessim,
RodriguezMias Ricard A.,
Gairí Margarida,
Giralt Ernest
Publication year - 2009
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.200900575
Subject(s) - tryptophan , side chain , heteronuclear single quantum coherence spectroscopy , chemistry , oligopeptidase , combinatorial chemistry , stereochemistry , computer science , nuclear magnetic resonance spectroscopy , biochemistry , organic chemistry , amino acid , enzyme , polymer
Be selective to simplify: An 15 N‐label is selectively incorporated into the tryptophan side chains of a large protein and a simplified [ 1 H, 15 N]‐TROSY HSQC spectrum is obtained without the need for deuteration.