The origin of the peculiar amide spectral features of proteins in aqueous solution is investigated, by exploiting a combined theoretical and experimental approach to UVRR spectra are recorded by tuning Synchrotron Radiation at several excitation wavelengths and modeled by using a recently developed multiscale protocol based on a polarizable QM/ MM approach. Thanks to the unparalleled agreement between theory and experiment, we demonstrate that specific hydrogen bond interactions, which dominate hydration dynamics around these solutes, play a crucial role in the selective enhancement of amide signals. These results further argue the capability of vibrational spectroscopy methods as valuable tools for refined structural analysis of peptides and proteins in aqueous solution.

Amide Spectral Fingerprints are Hydrogen Bonding-Mediated

Gómez, Sara
;
Egidi, Franco;Giovannini, Tommaso;Cappelli, Chiara
2022

Abstract

The origin of the peculiar amide spectral features of proteins in aqueous solution is investigated, by exploiting a combined theoretical and experimental approach to UVRR spectra are recorded by tuning Synchrotron Radiation at several excitation wavelengths and modeled by using a recently developed multiscale protocol based on a polarizable QM/ MM approach. Thanks to the unparalleled agreement between theory and experiment, we demonstrate that specific hydrogen bond interactions, which dominate hydration dynamics around these solutes, play a crucial role in the selective enhancement of amide signals. These results further argue the capability of vibrational spectroscopy methods as valuable tools for refined structural analysis of peptides and proteins in aqueous solution.
2022
Settore CHIM/02 - Chimica Fisica
DENSITY-FUNCTIONAL THEORY; RESONANCE RAMAN-SPECTRA; HYDRATION WATER; PRERESONANCE RAMAN; AQUEOUS SOLVATION; HERZBERG-TELLER; GAS-PHASE; DYNAMICS; PEPTIDES; DUSCHINSKY
   Horizon 2020
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11384/115886
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