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]
Producer: 20110712Description: 3713-23 p. digitalISSN:- 1520-4995
- Cryoelectron Microscopy -- methods
- Crystallography, X-Ray -- methods
- Dimerization
- Hordeum -- enzymology
- Magnesium -- chemistry
- Molecular Conformation
- Molecular Sequence Data
- NADP -- chemistry
- Oxidation-Reduction
- Peroxides -- chemistry
- Protein Conformation
- Protein Structure, Tertiary
- Recombinant Proteins -- chemistry
- Thioredoxin-Disulfide Reductase -- chemistry
- Thioredoxins -- chemistry
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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