NMR assignments of oxidised thioredoxin from Plasmodium falciparum

dc.creatorMunte, Claudia Elisabeth
dc.creatorBecker, Katja
dc.creatorSchirmer, Rolf Heiner
dc.creatorKalbitzer, Hans Robert
dc.date.accessioned2015-12-18T18:09:44Z
dc.date.accessioned2018-07-04T16:53:57Z
dc.date.available2015-12-18T18:09:44Z
dc.date.available2018-07-04T16:53:57Z
dc.date.created2015-12-18T18:09:44Z
dc.date.issued2009-12
dc.identifierBiomolecular NMR Assignments,Dordrecht : Springer Netherlands,v. 3, n. 2, p. 159-161, Dec. 2009
dc.identifier1874-2718
dc.identifierhttp://www.producao.usp.br/handle/BDPI/49368
dc.identifier10.1007/s12104-009-9163-7
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1641886
dc.description.abstractDuring 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
dc.languageeng
dc.publisherSpringer Netherlands
dc.publisherDordrecht
dc.relationBiomolecular NMR Assignments
dc.rightsrestrictedAccess
dc.subjectPlasmodium falciparum thioredoxin
dc.subjectCombined chemical shift
dc.subjectNMR resonance assignments
dc.titleNMR assignments of oxidised thioredoxin from Plasmodium falciparum
dc.typeArtículos de revistas


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