NMR assignments of oxidised thioredoxin from Plasmodium falciparum |
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Authors: | Claudia Elisabeth Munte Katja Becker Rolf Heiner Schirmer Hans Robert Kalbitzer |
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Institution: | 1. Institut für Biophysik und Physikalische Biochemie, Universit?t Regensburg, Universit?tsstr. 31, 93040, Regensburg, Germany 2. Interdiziplin?res Forschungszentrum, Universit?t Giessen, 35392, Giessen, Germany 3. Biochemie-Zentrum der Universit?t, 69120, Heidelberg, Germany
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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. |
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