Quantum behavior of water protons in protein hydration shell
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Updated: Jun 25, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
S E Pagnotta1, F Bruni, R Senesi
1Centro de Fisica des Materiales, Centro Mixto CSIC-UPV/EHU, Donostia-San Sebastian, Spain.
Abstract:
Quantum effects on the water proton dynamics over the surface of a hydrated protein are measured by means of broadband dielectric spectroscopy and deep inelastic neutron scattering. Dielectric spectroscopy indicates a reduced energy barrier for a hydrogenated protein sample compared to a deuterated one, along with a large and temperature-dependent isotopic ratio, in good agreement with theoretical studies. Recent deep inelastic neutron scattering data have been reanalyzed, and now show that the momentum distribution of water protons reflects a characteristic delocalization at ambient temperatures. These experimental findings might have far-reaching implications for enzymatic catalysis involving proton transfer processes, as in the case of the lysozyme protein studied in this report.
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