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Communication: Accurate determination of side-chain torsion angle χ1 in proteins: Phenylalanine residues

Author
Suardíaz, Reynier; Crespo-Otero, Rachel; De La Vega, José Manuel García; Pérez, Carlos; San Fabián Maroto, Jesúsuntranslated
Entity
UAM. Departamento de Química Física Aplicada
Publisher
AIP Publishing LLC
Date
2011-02-10
Citation
Journal of Chemical Physics 134.6 (2011): 061101
ISSN
0021-9606 (print); 1089-7690 (online)
DOI
10.1063/1.3553204
Funded by
Financial support from the MICINN of Spain (Project No. CTQ2007-66547 and CTQ2010-19232), the Comunidad de Madrid (Project Nos. S2009/ENE-1743) and AECID (Project No. D/023653/09) is gratefully acknowledged. Computational facilities have been provided by CCC-UAM
Project
Comunidad de Madrid. S2009/ENE-1743/RESTOENE
Editor's Version
http://dx.doi.org/10.1063/1.3553204
Subjects
Química
URI
http://hdl.handle.net/10486/665827
Note
The following article appeared in Journal of Chemical Physics 134.6 (2011): 061101 and may be found at http://scitation.aip.org/content/aip/journal/jcp/134/6/10.1063/1.3553204
Rights
© 2011 AIP Publishing LLC.

Abstract

Quantitative side-chain torsion angle χ1 determinations of phenylalanine residues in Desulfovibrio vulgaris flavodoxin are carried out using exclusively the correlation between the experimental vicinal coupling constants and theoretically determined Karplus equations. Karplus coefficients for nine vicinal coupling related with the torsion angle χ1 were calculated using the B3LYP functional and basis sets of different size. Optimized χ1 angles are in outstanding agreement with those previously reported by employing x ray and NMR measurements
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Google™ Scholar:Suardíaz, Reynier - Crespo-Otero, Rachel - De La Vega, José Manuel García - Pérez, Carlos - San Fabián Maroto, Jesús

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