Tarragó, Teresa <br/><br/>
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 
<br/><br/> Publication Type: Evaluation Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1439-7633 
<br/><br/><label>Standard No.: </label>10.1002/cbic.200900575  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Models, Molecular<br/>Nitrogen Isotopes--chemistry<br/>Nuclear Magnetic Resonance, Biomolecular--methods<br/>Prolyl Oligopeptidases<br/>Protein Structure, Tertiary<br/>Proteins--chemistry<br/>Research--economics<br/>Serine Endopeptidases--chemistry<br/>Tryptophan--chemistry