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.

Mots clés

Nuclear Magnetic Resonance Wheat Seed NOESY Spectrum Deuterated Water Wheat Storage Protein

Domaines

Sciences du Vivant [q-bio] Ingénierie des aliments

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https://hal.inrae.fr/hal-03745394

Soumis le : jeudi 4 août 2022-10:08:00

Dernière modification le : jeudi 3 août 2023-17:33:37

Dates et versions

hal-03745394 , version 1 (04-08-2022)

Identifiants

HAL Id : hal-03745394 , version 1
DOI : 10.1007/978-3-662-03720-1_9
PRODINRA : 131862

Citer

Frédéric F. de Lamotte, C Pruvost, Valerie Lullien Pellerin, Marie-Françoise Gautier, Philippe Joudrier, et al.. Structural Studies on Wheat Thioredoxin h. Conference on plant proteins from European crops. Food and non-food application, Nov 1996, Nantes, France. pp.5257, ⟨10.1007/978-3-662-03720-1_9⟩. ⟨hal-03745394⟩

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