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.