The relationship between the tyrosine residue 850–830 cm−1 Raman doublet intensity ratio and the aromatic side chain χ1 torsion angle

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Hernandez, B., Coic, Y.-M., Kruglik, S.-G., & Ghomi, M. (2024). The relationship between the tyrosine residue 850–830 cm−1 Raman doublet intensity ratio and the aromatic side chain χ1 torsion angle. Spectrochim Acta A Mol Biomol Spectrosc, 308, Article No. 123681. https://doi.org/10.1016/j.saa.2023.123681

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@article{Hernandez2024_487,
  author = {Hernandez, Belén and Coic, Yves-Marie and Kruglik, Sergei G. and Ghomi, Mahmoud},
  year = {2024},
  month = {3},
  title = {The relationship between the tyrosine residue 850–830 cm−1 Raman doublet intensity ratio and the aromatic side chain χ1 torsion angle},
  journal = {Spectrochim Acta A Mol Biomol Spectrosc},
  volume = {308},
  pages = {Article No. 123681},
  abstract = {Tyrosine (Tyr) residue in a peptide chain is characterized by the presence of seven Raman markers, referred to as Y(i) (i = 1, ..., 7), distributed over the middle wavenumber spectral region. Particularly, the changes observed in the relative intensity of Y(5) and Y(6) markers, appearing as a side by side doublet at ca. 850-830 cm(-1), has received a great attention. Primarily assigned to a Fermi-resonance effect between phenol ring planar and nonplanar modes, former density functional theory calculations led us to affiliate the Y(5)-Y(6) doublet to two distinct fundamental modes. Furthermore, despite the previous assumptions, it was evidenced that the reversal of the doublet intensity ratio cannot be solely explained by hydrogen bonding on the phenol hydroxyl group involved in Tyr. Herein, upon analyzing the observed and theoretical data collected from the cationic species of the tripeptide Gly-Tyr-Gly, the crucial effect of the aromatic side chain orientation, especially that of the chi(1) torsion angle defined around the C(alpha)C(beta) bond, on the Tyr doublet intensity ratio has been evidenced.},
  url = {https://www.sciencedirect.com/science/article/abs/pii/S1386142523013665},
  doi = {10.1016/j.saa.2023.123681},
}

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TY  - JOUR
AU  - Hernandez, Belén
AU  - Coic, Yves-Marie
AU  - Kruglik, Sergei G.
AU  - Ghomi, Mahmoud
PY  - 2024
DA  - 2024/03/05
TI  - The relationship between the tyrosine residue 850–830 cm−1 Raman doublet intensity ratio and the aromatic side chain χ1 torsion angle
JO  - Spectrochim Acta A Mol Biomol Spectrosc
VL  - 308
AB  - Tyrosine (Tyr) residue in a peptide chain is characterized by the presence of seven Raman markers, referred to as Y(i) (i = 1, ..., 7), distributed over the middle wavenumber spectral region. Particularly, the changes observed in the relative intensity of Y(5) and Y(6) markers, appearing as a side by side doublet at ca. 850-830 cm(-1), has received a great attention. Primarily assigned to a Fermi-resonance effect between phenol ring planar and nonplanar modes, former density functional theory calculations led us to affiliate the Y(5)-Y(6) doublet to two distinct fundamental modes. Furthermore, despite the previous assumptions, it was evidenced that the reversal of the doublet intensity ratio cannot be solely explained by hydrogen bonding on the phenol hydroxyl group involved in Tyr. Herein, upon analyzing the observed and theoretical data collected from the cationic species of the tripeptide Gly-Tyr-Gly, the crucial effect of the aromatic side chain orientation, especially that of the chi(1) torsion angle defined around the C(alpha)C(beta) bond, on the Tyr doublet intensity ratio has been evidenced.
SP  - Article No. 123681
DO  - 10.1016/j.saa.2023.123681
UR  - https://www.sciencedirect.com/science/article/abs/pii/S1386142523013665
ER  -