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00925njm 22002777a 4500 dc Suardíaz Delrío, Reynier author Crespo-Otero, Rachel author Pérez, Christine author San Fabián, Jesús author García de la Vega, José Manuel author 2011 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 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 0021-9606 10.1063/1.3553204 https://hdl.handle.net/20.500.14352/92505 1089-7690 https://doi.org/10.1063/1.3553204 Communication: Accurate determination of side-chain torsion angle χ1 in proteins: Phenylalanine residues