Communication: Accurate determination of side-chain torsion angle χ1 in proteins: Phenylalanine residues
Loading...
Official URL
Full text at PDC
Publication date
2011
Advisors (or tutors)
Editors
Journal Title
Journal ISSN
Volume Title
Publisher
American Institute of Physics
Citations
Exportar
Citation
R. Suardíaz, R. Crespo-Otero, C. Pérez, J. San Fabián, J. M. García de la Vega; Communication: Accurate determination of side-chain torsion angle χ1 in proteins: Phenylalanine residues. J. Chem. Phys. 14 February 2011; 134 (6): 061101. https://doi.org/10.1063/1.3553204
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