A Cost‐Effective Labeling Strategy for the NMR Study of Large Proteins: Selective  15 N‐Labeling of the Tryptophan Side Chains of Prolyl Oligopeptidase | Zendy

Tarragó Teresa | Zendy; Claasen Birgit | Zendy; Kichik Nessim | Zendy; RodriguezMias Ricard A. | Zendy; Gairí Margarida | Zendy; Giralt Ernest | Zendy

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research