Accurate determination of side-chain torsion angle χ1 in proteins: Phenylalanine residues

R. Suardíaz; R. Crespo‑Otero; C. Pérez; J. San Fabián; J. M. García de la Vega

doi:10.1063/1.3553204

Accurate determination of side-chain torsion angle χ1 in proteins: Phenylalanine residues

R. Suardíaz, R. Crespo‑Otero, C. Pérez, J. San Fabián, J. M. García de la Vega

Chemistry

Queen Mary University of London

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

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.

Original language	English
Number of pages	4
Journal	Journal of Chemical Physics
Volume	134
Issue number	061101
Early online date	10 Feb 2011
DOIs	https://doi.org/10.1063/1.3553204
Publication status	E-pub ahead of print - 10 Feb 2011

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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.",

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T2 - Phenylalanine residues

AU - Suardíaz, R.

AU - Crespo‑Otero, R.

AU - Pérez, C.

AU - San Fabián, J.

AU - García de la Vega, J. M.

PY - 2011/2/10

Y1 - 2011/2/10

N2 - 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.

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.

U2 - 10.1063/1.3553204

DO - 10.1063/1.3553204

M3 - Article

SN - 0021-9606

VL - 134

JO - Journal of Chemical Physics

JF - Journal of Chemical Physics

IS - 061101

ER -

Accurate determination of side-chain torsion angle χ1 in proteins: Phenylalanine residues

Abstract

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