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.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Munte CE,Becker K,Schirmer RH,Kalbitzer HRdoi
10.1007/s12104-009-9163-7subject
Has Abstractpub_date
2009-12-01 00:00:00pages
159-61issue
2eissn
1874-2718issn
1874-270Xjournal_volume
3pub_type
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journal_title:Biomolecular NMR assignments
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