Structural Studies on Wheat Thioredoxin h
Triticum aestivum thioredoxin h overproduced in Escherichia coli (TrxTa) was purified to homogeneity. TrxTa showed a lower stability than other thioredoxins but was active and exhibited the same reactivity as wheat seed isolated thioredoxin h. Nuclear magnetic resonance and modeling studies revealed a canonical thioredoxin fold.
KeywordsNuclear Magnetic Resonance Wheat Seed NOESY Spectrum Deuterated Water Wheat Storage Protein
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