Please use this identifier to cite or link to this item: http://hdl.handle.net/2307/383
Title: Quantum Behavior of Water Protons in Protein Hydration Shell
Authors: Pagnotta, S. E.
Bruni, Fabio
Senesi, R.
Pietropaolo, A.
Keywords: INELASTIC NEUTRON-SCATTERING
ENZYME CATALYSIS
HYDROGEN-BONDS
DYNAMICS
TRANSITION
TIME
FLUCTUATIONS
DEPENDENCE
LYSOZYME
SOLVENT
Issue Date: Mar-2009
Publisher: Elsevier (Cell Press)
Abstract: Quantum effects on the water proton dynamics over the surface of ahydrated protein are measured by means of broadband dielectricspectroscopy and deep inelastic neutron scattering. Dielectricspectroscopy indicates a reduced energy barrier for a hydrogenatedprotein sample compared to a deuterated one, along with a large andtemperature-dependent isotopic ratio, in good agreement withtheoretical studies. Recent deep inelastic neutron scattering data havebeen reanalyzed, and now show that the momentum distribution of waterprotons reflects a characteristic delocalization at ambienttemperatures. These experimental findings might have far-reachingimplications for enzymatic catalysis involving proton transferprocesses, as in the case of the lysozyme protein studied in thisreport.
URI: http://hdl.handle.net/2307/383
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2008.10.062
Appears in Collections:A - Articolo su rivista
X_Dipartimento di Fisica 'Edoardo Amaldi'

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