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1H, 13C and 15N chemical shift assignments of the thioredoxin from the obligate anaerobe Desulfovibrio vulgaris Hildenborough

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Abstract

Thioredoxins are ubiquitous key antioxidant enzymes which play an essential role in cell defense against oxidative stress. They maintain the redox homeostasis owing to the regulation of thiol-disulfide exchange. In the present paper, we report the full resonance assignments of 1H, 13C and 15N atoms for the reduced and oxidized forms of Desulfovibrio vulgaris Hildenborough thioredoxin 1 (Trx1). 2D and 3D heteronuclear NMR experiments were performed using uniformly 15N-, 13C-labelled Trx1. Chemical shifts of 97% of the backbone and 90% of the side chain atoms were obtained for the oxidized and reduced form (BMRB deposits with accession number 17299 and 17300, respectively).

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Authors and Affiliations

  1. IMR–IFR88, CNRS; Aix-Marseille Université, Marseille, France

    Edwige B. Garcin, Olivier Bornet, Laetitia Pieulle, Françoise Guerlesquin & Corinne Sebban-Kreuzer

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  1. Edwige B. Garcin
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  2. Olivier Bornet
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  3. Laetitia Pieulle
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  4. Françoise Guerlesquin
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  5. Corinne Sebban-Kreuzer
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Correspondence to Françoise Guerlesquin.

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Garcin, E.B., Bornet, O., Pieulle, L. et al. 1H, 13C and 15N chemical shift assignments of the thioredoxin from the obligate anaerobe Desulfovibrio vulgaris Hildenborough. Biomol NMR Assign 5, 177–179 (2011). https://doi.org/10.1007/s12104-011-9294-5

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  • DOI: https://doi.org/10.1007/s12104-011-9294-5

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