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dc.contributor.author
Neira, José L.
dc.contributor.author
González, Carlos
dc.contributor.author
Toiron, Catherine
dc.contributor.author
de Prat Gay, Gonzalo
dc.contributor.author
Rico, Manuel
dc.date.available
2018-05-15T15:25:36Z
dc.date.issued
2001-12
dc.identifier.citation
Neira, José L.; González, Carlos; Toiron, Catherine; de Prat Gay, Gonzalo; Rico, Manuel; Three-Dimensional Solution Structure and Stability of Thioredoxin m from Spinach †; American Chemical Society; Biochemistry; 40; 50; 12-2001; 15246-15256
dc.identifier.issn
0006-2960
dc.identifier.uri
http://hdl.handle.net/11336/45197
dc.description.abstract
Proton NMR spectral resonances of thioredoxin m from spinach have been assigned, and its solution structure has been determined on the basis of 1156 nuclear Overhauser effect- (NOE-) derived distance constraints by using restrained molecular dynamics calculations. The average pairwise root-mean-square deviation (RMSD) for the 25 best NMR structures for the backbone was 1.0 +/- 0.1, when the structurally well-defined residues were considered. The N- and C-terminal segments (1-13 and 118-119) and residues 41-49, comprising the active site, are highly disordered. At the time of concluding this work, a crystal structure of this protein was reported, in which thioredoxin m was found to crystallize as noncovalent dimers. Although the solution and crystal structures are very similar, no evidence was found about the existence of dimers in solution, thus confirming that dimerization is not needed for the regulatory activity of thioredoxin m. The spinach thioredoxin m does not unfold by heat in the range 25-85 degrees C, as revealed by thermal circular dichroic (CD) measurements. However, its unfolding free energy (9.1 +/- 0.8 kcal mol(-1), at pH 5.3 and 25 degrees C) could be determined by extrapolating the free energy values obtained at different concentrations of guanidinium chloride (GdmCl). The folding-unfolding process is two-state as indicated by the coincidence of the CD denaturation curves obtained at far and near UV. The H/D exchange behavior of backbone amide protons was analyzed. The slowest-exchanging protons, requiring a global-unfolding mechanism in order to exchange, are those from beta2, beta3, and beta4, the central strands of the beta-sheet, which constitute the main element of the core of the protein. The free energies obtained from exchange measurements of protons belonging to the alpha-helices are lower than those derived from GdmCl denaturation studies, indicating that those protons exchange by local-unfolding mechanisms.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Chemical Society
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Thioredoxin
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Protein Structure
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Protein Folding
dc.subject.classification
Otras Ciencias Químicas
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Ciencias Químicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Three-Dimensional Solution Structure and Stability of Thioredoxin m from Spinach †
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-05-10T15:45:17Z
dc.identifier.eissn
1520-4995
dc.journal.volume
40
dc.journal.number
50
dc.journal.pagination
15246-15256
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Washington
dc.description.fil
Fil: Neira, José L.. Universidad de Miguel Hernández; España
dc.description.fil
Fil: González, Carlos. Consejo Superior de Investigaciones Científicas; España
dc.description.fil
Fil: Toiron, Catherine. Consejo Superior de Investigaciones Científicas; España
dc.description.fil
Fil: de Prat Gay, Gonzalo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
dc.description.fil
Fil: Rico, Manuel. Consejo Superior de Investigaciones Científicas; España
dc.journal.title
Biochemistry
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/abs/10.1021/bi011186x
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/bi011186x


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