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.
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