1. RODNA
  2. CONICET
  3. CONICET
Registro completo de metadatos
Campo DC Valor Lengua/Idioma
dc.provenanceCONICET-
dc.creatorVila, Jorge Alberto-
dc.creatorSerrano, P.-
dc.creatorWüthrich, Kurt-
dc.creatorScheraga, Harold-
dc.date2017-04-18T22:14:18Z-
dc.date2017-04-18T22:14:18Z-
dc.date2010-09-
dc.date2017-04-18T14:26:39Z-
dc.date.accessioned2019-04-29T15:44:21Z-
dc.date.available2019-04-29T15:44:21Z-
dc.date.issued2017-04-18T22:14:18Z-
dc.date.issued2017-04-18T22:14:18Z-
dc.date.issued2010-09-
dc.date.issued2017-04-18T14:26:39Z-
dc.identifierVila, Jorge Alberto; Serrano, P.; Wüthrich, Kurt; Scheraga, Harold; Sequential nearest-neighbor effects on computed 13Cα chemical shifts; Springer; Journal Of Biomolecular Nmr; 48; 1; 9-2010; 23-30-
dc.identifier0925-2738-
dc.identifierhttp://hdl.handle.net/11336/15433-
dc.identifier1573-5001-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/300757-
dc.descriptionTo evaluate sequential nearest-neighbor effects on quantum-chemical calculations of 13Cα chemical shifts, we selected the structure of the nucleic acid binding (NAB) protein from the SARS coronavirus determined by NMR in solution (PDB id 2K87). NAB is a 116-residue α/β protein, which contains 9 prolines and has 50% of its residues located in loops and turns. Overall, the results presented here show that sizeable nearest-neighbor effects are seen only for residues preceding proline, where Pro introduces an overestimation, on average, of 1.73 ppm in the computed 13Cα chemical shifts. A new ensemble of 20 conformers representing the NMR structure of the NAB, which was calculated with an input containing backbone torsion angle constraints derived from the theoretical 13Cα chemical shifts as supplementary data to the NOE distance constraints, exhibits very similar topology and comparable agreement with the NOE constraints as the published NMR structure. However, the two structures differ in the patterns of differences between observed and computed 13Cα chemical shifts, Δca,i, for the individual residues along the sequence. This indicates that the Δca,i -values for the NAB protein are primarily a consequence of the limited sampling by the bundles of 20 conformers used, as in common practice, to represent the two NMR structures, rather than of local flaws in the structures.-
dc.descriptionFil: Vila, Jorge Alberto. Cornell University; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto de Matemática Aplicada de San Luis; Argentina. Universidad Nacional de San Luis; Argentina-
dc.descriptionFil: Serrano, P.. The Scripps Research Institute; Estados Unidos-
dc.descriptionFil: Wüthrich, Kurt. The Scripps Research Institute; Estados Unidos-
dc.descriptionFil: Scheraga, Harold. Cornell University; Estados Unidos-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherSpringer-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s10858-010-9435-7-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10858-010-9435-7-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.source.urihttp://hdl.handle.net/11336/15433-
dc.subjectQuantum-chemical calculation of 13Cα- chemical shifts-
dc.subjectNMR structures of proteins-
dc.subjectSampling of conformation space-
dc.subjectFísica Atómica, Molecular y Química-
dc.subjectCiencias Físicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleSequential nearest-neighbor effects on computed 13Cα chemical shifts-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
Aparece en las colecciones: CONICET

Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Mostrar el registro sencillo del ítem