Wulff, Ragna Peterson <br/><br/>
The activity of barley NADPH-dependent thioredoxin reductase C is independent of the oligomeric state of the protein: tetrameric structure determined by cryo-electron microscopy.  [electronic resource] 

 -  Biochemistry  May 2011 
 - 3713-23 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1520-4995 
<br/><br/><label>Standard No.: </label>10.1021/bi200058a  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Cryoelectron Microscopy--methods<br/>Crystallography, X-Ray--methods<br/>Dimerization<br/>Hordeum--enzymology<br/>Magnesium--chemistry<br/>Molecular Conformation<br/>Molecular Sequence Data<br/>NADP--chemistry<br/>Oxidation-Reduction<br/>Peroxides--chemistry<br/>Protein Conformation<br/>Protein Structure, Tertiary<br/>Recombinant Proteins--chemistry<br/>Thioredoxin-Disulfide Reductase--chemistry<br/>Thioredoxins--chemistry