Neutron
scattering explains how myoglobin can perform without water
Understanding
will help protein’s potential application in biochemical gas sensors or in
state-of-the-art wound dressing.
Proteins do
not need to be surrounded by water to carry out their vital biological
functions, according to scientists from the Institut de Biologie Structurale
(IBS) in Grenoble, the University of Bristol, the Australian National
University, the Forschungszentrum Jülich, in Germany and the ILL. In a new
paper published in the Journal of the American Chemical Society, the team used
a state of the art neutron scattering technique to demonstrate that when
myoglobin, an oxygen-binding protein found in the muscle tissue of vertebrates,
is enclosed in a sheath of surfactant molecules, it moves in the same way as when it is
surrounded by water. These motions are essential if a protein is to perform its
biological function, and their findings make proteins a viable material for use
in new wound dressings or even as chemical gas sensors.