Chemical shift assignments of the canecystatin-1 from Saccharum officinarum

dc.creatorCavini, Ítalo Augusto
dc.creatorSilva, Rodrigo de Oliveira
dc.creatorMarques, Ivo de Almeida
dc.creatorKalbitzer, Hans Robert
dc.creatorMunte, Claudia Elisabeth
dc.date.accessioned2014-05-28T17:33:38Z
dc.date.accessioned2018-07-04T16:46:53Z
dc.date.available2014-05-28T17:33:38Z
dc.date.available2018-07-04T16:46:53Z
dc.date.created2014-05-28T17:33:38Z
dc.date.issued2013-10
dc.identifierBiomolecular NMR Assignments, Dordrecht : Springer, v. 7, n. 2, p. 163-165, Oct. 2013
dc.identifier1874-2718
dc.identifierhttp://www.producao.usp.br/handle/BDPI/45089
dc.identifier10.1007/s12104-012-9401-2
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1640276
dc.description.abstractCystatins are cysteine proteases inhibitors that are widely distributed among insects, mammalians and plants. Here we report the complete resonance assignment of canecystatin-1 from Saccharum officinarum obtained by heteronuclear multidimensional high-resolution nuclear magnetic resonance spectroscopy. The consensus chemical shift index was calculated and showed the presence of one α-helix (residues 27-43) and three β-strands (residues 48-74, 78-89 and 94-104), a secondary structure pattern that suggests a domain-swapped structure as presented by stefin B and human cystatin C, opposed to the monomeric structure yet found in other phytocystatins like oryza and pineapple cystatin.
dc.languageeng
dc.publisherSpringer
dc.publisherDordrecht
dc.relationBiomolecular NMR Assignments
dc.rightsCopyright Springer Science+Business Media B.V.
dc.rightsrestrictedAccess
dc.subjectSaccharum officinarum cystatin
dc.subjectCanecystatin-1
dc.subjectPhytocystatin
dc.subjectCysteine protease inhibitor
dc.titleChemical shift assignments of the canecystatin-1 from Saccharum officinarum
dc.typeArtículos de revistas


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