Mañana, JUEVES, 24 DE ABRIL, el sistema se apagará debido a tareas habituales de mantenimiento a partir de las 9 de la mañana. Lamentamos las molestias.
Searching conformational analysis of Asp residues through theoretical ³J vicinal coupling constants and Karplus equations
Entity
UAM. Departamento de Química Física AplicadaPublisher
WileyDate
2022-07-09Citation
10.1002/qua.26979
International Journal of Quantum Chemistry 122.21 (2022): e26979
ISSN
0020-7608 (print); 1097-461X (online)DOI
10.1002/qua.26979Editor's Version
https://doi.org/10.1002/qua.26979Subjects
Asp dipeptide model; Density functional theory; Karplus equations; Side-chain conformation; Spin–spin coupling constants; Física; QuímicaRights
© 2022 The AuthorsAbstract
The dependence of the vicinal spin–spin coupling constants on the torsion side chain angle χ1 through the Karplus equations is considered for the study of the structure of Asp amino acid residues. Experimental and theoretical, obtained with density functional theory methods, vicinal coupling constants combined with extended Karplus equations, which include six coefficients, are applied to a dipeptide model of the amino acid Asp. To find out the empirical χ1 angles of the side chain, a statistical analysis procedure is developed to compute the rmsd values and find the χ1 as the minimum of those values. The χ1 values obtained in this work for nine Asp residues of the flavodoxin protein Desulfovibrio vulgaris are successfully compared with those derived by nuclear magnetic resonance and X-rays
Files in this item
Google Scholar:Botella, María
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Ema López, Ignacio de
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San Fabián Maroto, Jesús
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García de la Vega, José Manuel
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