Journal article

Publication year: 2009

Pages: 159-161

Journal: Biomolecular NMR Assignments

Volume number: 3

Issue number: 2

ISSN: 1874-2718

eISSN: 1874-270X

DOI Link: https://doi.org/10.1007/s12104-009-9163-7

Publisher: Springer

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.

Harvard Citation style: Munte, C., Becker, K., Schirmer, R. and Kalbitzer, H. (2009) NMR assignments of oxidised thioredoxin from Plasmodium falciparum, Biomolecular NMR Assignments, 3(2), pp. 159-161. https://doi.org/10.1007/s12104-009-9163-7

APA Citation style: Munte, C., Becker, K., Schirmer, R., & Kalbitzer, H. (2009). NMR assignments of oxidised thioredoxin from Plasmodium falciparum. Biomolecular NMR Assignments. 3(2), 159-161. https://doi.org/10.1007/s12104-009-9163-7