A cost-effective labeling strategy for the NMR study of large proteins: selective 15N-labeling of the tryptophan side chains of prolyl oligopeptidase.

Tarragó, Teresa

A cost-effective labeling strategy for the NMR study of large proteins: selective 15N-labeling of the tryptophan side chains of prolyl oligopeptidase. [electronic resource] - Chembiochem : a European journal of chemical biology Nov 2009 - 2736-9 p. digital

Publication Type: Evaluation Study; Journal Article; Research Support, Non-U.S. Gov't

1439-7633

10.1002/cbic.200900575 doi


Animals
Models, Molecular
Nitrogen Isotopes--chemistry
Nuclear Magnetic Resonance, Biomolecular--methods
Prolyl Oligopeptidases
Protein Structure, Tertiary
Proteins--chemistry
Research--economics
Serine Endopeptidases--chemistry
Tryptophan--chemistry