New research by scientists at the University of Bristol has challenged one of the key beliefs in chemistry: that proteins are dependent on water to survive and function. The team’s findings, published in Chemical Science (doi: 10.1039/C2SC20143G), could eventually lead to the development of new industrial enzymes.
It is generally thought that proteins are dependent on water to survive and function. Previously, it was thought that water was essential to the refolding of proteins after denaturation, however, the Bristol findings suggest this isn’t necessarily the case. Using circular dichroism, Dr Adam Perriman of Bristol’s School of Chemistry and colleagues have shown that the oxygen-carrying protein myoglobin can refold in an environment that is almost completely devoid of water molecules.
Dr Perriman said: “We achieved this by attaching polymer molecules to the surface of the protein and then removing the water to give a viscous liquid which, when cooled from a temperature as high as 155°C, refolded back to its original structure. We then used the Circular Dichroism beamline (B23) at Diamond Light Source, the UK’s national synchrotron science facility in Oxfordshire, to track the refolding of the myoglobin structure and were astounded when we became aware of the extremely high thermal resistance of the new material.”
These findings could pave the way for the development of new industrial enzymes where hyper-thermal resistance would play a crucial role, in applications ranging from biosensor development to electrochemical reduction of CO2 to liquid fuels.
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