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oai:docta.ucm.es:20.500.14352/925052025-03-18T12:55:17Zcom_20.500.14352_14col_20.500.14352_15

Communication: Accurate determination of side-chain torsion angle χ1 in proteins: Phenylalanine residues Suardíaz Delrío, Reynier Crespo-Otero, Rachel Pérez, Christine San Fabián, Jesús García de la Vega, José Manuel 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 2024-01-11T11:36:06Z 2024-01-11T11:36:06Z 2024-01-11T11:36:06Z 2011 journal article https://hdl.handle.net/20.500.14352/92505 0021-9606 10.1063/1.3553204 1089-7690 eng info:eu-repo/grantAgreement/MEC//CTQ2007-66547/ES/DESARROLLO Y EVALUACION DE ELECTROCATALIZADORES PARA USO COMO CATODOS EN CELDAS DE COMBUSTIBLE TIPO PEM/ info:eu-repo/grantAgreement/MICINN//CTQ2010-19232/ES/ESTRUCTURA ELECTRONICA MOLECULAR: METODOLOGIA Y APLICACIONES/ info:eu-repo/grantAgreement/CAM//S2009%2FENE-1743/ES/Producción de combustibles limpios para transporte a partir de residuos agro%2Fforestales y oleaginosos/ D/023653/09 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 http://creativecommons.org/licenses/by-nc-nd/4.0/ open access Attribution-NonCommercial-NoDerivatives 4.0 International American Institute of Physics