Proton momentum distribution in a protein hydration shell

The momentum distribution of protons in the hydration shell of a globular protein has been measured through deep inelastic neutron scattering at 180 and 290 K, below and above the crossover temperature Tc=1.23Tg, where Tg=219 K is the glass transition temperature. It is found that the mean kinetic e...

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Veröffentlicht in:Physical review letters 2007-03, Vol.98 (13), p.138102-138102, Article 138102
Hauptverfasser: Senesi, R, Pietropaolo, A, Bocedi, A, Pagnotta, S E, Bruni, F
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container_end_page 138102
container_issue 13
container_start_page 138102
container_title Physical review letters
container_volume 98
creator Senesi, R
Pietropaolo, A
Bocedi, A
Pagnotta, S E
Bruni, F
description The momentum distribution of protons in the hydration shell of a globular protein has been measured through deep inelastic neutron scattering at 180 and 290 K, below and above the crossover temperature Tc=1.23Tg, where Tg=219 K is the glass transition temperature. It is found that the mean kinetic energy of the water hydrogens shows no temperature dependence, but the measurements are accurate enough to indicate a sensible change of momentum distribution and effective potential felt by protons, compatible with the transition from a single to a double potential well. This could support the presence of tunneling effects even at room temperature, playing an important role in biological function.
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ispartof Physical review letters, 2007-03, Vol.98 (13), p.138102-138102, Article 138102
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language eng
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source MEDLINE; American Physical Society Journals
subjects Algorithms
DEEP INELASTIC SCATTERING
GLASS
HYDRATION
HYDROGEN
KINETIC ENERGY
MATERIALS SCIENCE
NEUTRON DIFFRACTION
Neutrons
POTENTIALS
PROTEINS
Proteins - chemistry
PROTONS
Scattering, Radiation
Temperature
TEMPERATURE DEPENDENCE
TEMPERATURE RANGE 0065-0273 K
TEMPERATURE RANGE 0273-0400 K
TRANSITION TEMPERATURE
TUNNEL EFFECT
WATER
Water - chemistry
title Proton momentum distribution in a protein hydration shell
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