RT Journal Article
T1 Communication: Accurate determination of side-chain torsion angle χ1 in proteins: Phenylalanine residues
A1 Suardíaz Delrío, Reynier
A1 Crespo-Otero, Rachel
A1 Pérez, Christine
A1 San Fabián, Jesús
A1 García de la Vega, José Manuel
AB 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
PB American Institute of Physics
SN 0021-9606
YR 2011
FD 2011
LK https://hdl.handle.net/20.500.14352/92505
UL https://hdl.handle.net/20.500.14352/92505
LA eng
NO 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
NO Ministerio de Ciencia e Innovación (España)
NO Agencia Española de Cooperación Internacional para el Desarrollo
NO Comunidad de Madrid
DS Docta Complutense
RD 11 abr 2025