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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


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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)