Mostrar el registro sencillo del ítem

dc.contributor.author
Vila, Jorge Alberto
dc.contributor.author
Serrano, P.
dc.contributor.author
Wüthrich, Kurt
dc.contributor.author
Scheraga, Harold
dc.date.available
2017-04-18T22:14:18Z
dc.date.issued
2010-09
dc.identifier.citation
Vila, 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.identifier.issn
0925-2738
dc.identifier.uri
http://hdl.handle.net/11336/15433
dc.description.abstract
To 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.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Quantum-Chemical Calculation of 13cα- Chemical Shifts
dc.subject
Nmr Structures of Proteins
dc.subject
Sampling of Conformation Space
dc.subject.classification
Física Atómica, Molecular y Química
dc.subject.classification
Ciencias Físicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Sequential nearest-neighbor effects on computed 13Cα chemical shifts
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-04-18T14:26:39Z
dc.identifier.eissn
1573-5001
dc.journal.volume
48
dc.journal.number
1
dc.journal.pagination
23-30
dc.journal.pais
Países Bajos
dc.journal.ciudad
Ámsterdam
dc.description.fil
Fil: 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.description.fil
Fil: Serrano, P.. The Scripps Research Institute; Estados Unidos
dc.description.fil
Fil: Wüthrich, Kurt. The Scripps Research Institute; Estados Unidos
dc.description.fil
Fil: Scheraga, Harold. Cornell University; Estados Unidos
dc.journal.title
Journal Of Biomolecular Nmr
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s10858-010-9435-7
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10858-010-9435-7


Archivos asociados

Documento no disponible

Comunidades y colecciones

Mostrar el registro sencillo del ítem