Munte, Claudia Elisabeth and Becker, Katja and Schirmer, Rolf Heiner and Kalbitzer, Hans Robert (2009) NMR assignments of oxidised thioredoxin from Plasmodium falciparum. BIOMOLECULAR NMR ASSIGNMENTS, 3 (2). pp. 159-161. ISSN 1874-2718,
Full text not available from this repository. (Request a copy)Abstract
During its life cycle, the malaria parasite Plasmodium falciparum is found intracellular to human erythrocytes, where its survival and ability to multiply critically depends on the control of the environment redox state. Thioredoxin is a small protein containing 104 amino acids that is part of the parasite specific redox system. During the catalytic cycle it alternates between a reduced and oxidised form. Here we report the complete resonance assignment of Plasmodium falciparum thioredoxin in its oxidized form by heteronuclear multidimensional spectroscopy. The obtained chemical shifts differ significantly from those reported earlier for this protein in its reduced state.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PROTEINS; SYSTEM; REDOX; Plasmodium falciparum thioredoxin; Combined chemical shift; NMR resonance assignments |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 27 Aug 2020 12:19 |
| Last Modified: | 27 Aug 2020 12:19 |
| URI: | https://pred.uni-regensburg.de/id/eprint/28001 |
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