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Story Tip
This is a story idea from the Department of Energy’s Oak Ridge
National Laboratory. To arrange for an interview with a researcher,
please contact the Communications and External Relations staff
member identified at the end of the tip.
Proteins’ biological functions, such as the ability to
metabolize drugs in our bodies, are known to rely heavily on the
presence of water, but mechanisms behind the relationship have
remained unclear. In a paper published in Physical Review Letters,
researchers from Oak Ridge National Laboratory have provided new
evidence that suggests water is even more involved in protein
dynamics than previously thought. Through a novel combination of
supercomputer simulations and neutron scattering experiments, the
research team found that the effects of water reach into the very
core of a protein instead of remaining on the surface, as earlier
research had suggested. “The implications are that surface
hydration may lubricate dynamics in interior protein active sites,
thus enabling biological function,” said lead author Jeremy
Smith.
