Then they used a neutron-scattering technique to observe how well the proteins could move, a measure of their proper functioning. They found that the protein-polymer hybrids moved as well as proteins in water, remaining flexible and exhibiting the usual internal dynamics. Importantly, they could still bind oxygen as well as myoglobin does in living tissue. The finding overturns the dogma that water is the most important biological molecule.

Previous studies have shown that modifying proteins with polymers can lead to therapeutic applications. For example, applying a polyethylene glycol (PEG) coating - a process known as PEGylation - can mask a protein and help it avoid rejection by the immune system. But where previous studies have required some kind of solvent for the protein to function, the Bristol team were able to observe proteins functioning normally in an entirely solvent-free environment.

Among the applications the team intends to explore are wound dressings in which the liquid protein is applied like a paste. It could then act like an oxygen pump, with a chemical reaction between the protein layer and a glucose membrane drawing oxygen down through the dressing to the surface of the skin.