Journal
PHYSICAL REVIEW LETTERS
Volume 98, Issue 13, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.98.138102
Keywords
-
Categories
Ask authors/readers for more resources
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 T-c=1.23T(g), where T-g=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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available