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Structural Studies on Wheat Thioredoxin h

  • F. de Lamotte-Guery
  • C. Pruvost
  • V. Lullien-Pellerin
  • M.-F. Gautier
  • P. Joudrier
  • M.-A. Delsuc

Summary

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.

Keywords

Nuclear Magnetic Resonance Wheat Seed NOESY Spectrum Deuterated Water Wheat Storage Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • F. de Lamotte-Guery
    • 1
  • C. Pruvost
    • 2
  • V. Lullien-Pellerin
    • 1
  • M.-F. Gautier
    • 1
  • P. Joudrier
    • 1
  • M.-A. Delsuc
    • 2
  1. 1.INRA Unité de Biochimie et Biologie Moléculaire des Céréalesontpellier Cédex 01France
  2. 2.CNRS, INSERM., Centre de Biochimie Structurale - UMR C 9955Université Montpellier IMontpellierFrance

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