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

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 (1)H, (13)C and (15)N atoms for the reduced and oxidized forms of Desulfovibrio vulgaris Hildenborough thioredoxin 1 (Trx1). 2D and 3D heteronuclear NMR experiments were performed using uniformly (15)N-, (13)C-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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https://hal.archives-ouvertes.fr/hal-01458276
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Submitted on : Monday, February 6, 2017 - 5:49:28 PM
Last modification on : Tuesday, October 19, 2021 - 10:58:53 PM

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Edwige B Garcin, Olivier Bornet, Laetitia Pieulle, Françoise Guerlesquin, Corinne Sebban-Kreuzer. 1H, 13C and 15N chemical shift assignments of the thioredoxin from the obligate anaerobe Desulfovibrio vulgaris Hildenborough.. Biomol NMR Assign, 2011, 5 (2), pp.177--9. ⟨10.1007/s12104-011-9294-5⟩. ⟨hal-01458276⟩

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