Proteins consist of one or more polypeptides, chains of amino acids held together by peptide bonds. If a protein in water is heated to temperatures approaching the boiling point of water, these chains will lose their structure and the protein will denature (unfold).
A more clear example of denaturing/unfolding occurs when an egg is hard-boiled: the structures of the proteins in the egg unfold with temperature and stick together creating a solid. In the egg's case, the process cannot be reversed but there are many examples where cooling the protein results in refolding of the structure. Proteins also evolved in a water-rich environment so it is generally accepted that they are dependent on water to survive and function, like in the refolding process, however some new findings suggest this isn't necessarily the case.
Using circular dichroism, a spectroscopic technique, 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.
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."
The results 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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