A protein folds to assume its functional shape. It has been thought that water is essential to this process. But the Bristol team’s results, which were recently published in the journal Chemical Science, suggest that this isn’t necessarily the case.
“We were able to show that myoglobin can refold in an environment that is almost completely devoid of water molecules. 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 used beamline B23 at the Diamond synchrotron 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.”
Dr Adam Perriman, University of Bristol
Diamond Light Source is the UK's national synchrotron science facility, located at the Harwell Science and Innovation Campus in Oxfordshire.
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