How (and why) chemists figured out how to unboil an egg

Jan. 30, 2015

You can't unscramble an egg. But you can unboil it. That's what chemists at University of California, Irvine, and South Australia’s Flinders University have done; their findings were recently published in the journal ChemBioChem.

Gregory Weiss, PhD, professor of chemistry and molecular biology, wanted to figure out how to refold lab-created proteins associated with cancer. “The problem is when we tried to produce cancer-associated proteins… often times the proteins come out as a jumbled mess,” Weiss says. It can take days, even weeks, for scientists to tease out those gunked-up proteins that are stuck to the edges of test tubes. On a visit to South Australia’s Flinders University laboratory Weiss witnessed a high-powered, vortex-fluid device that essentially pulls things apart, Weiss thought: why not pull proteins apart?

The Chemists took an egg and separated the yolk from the white. The whites were boiled for 20 minutes at 90 degrees Celsius. “At the end they're rock hard,” Weiss says. The egg whites' proteins had changed shape, but the proteins themselves remained intact — much like misshapen cancer-associated proteins. Weiss unfolded those egg white proteins back into shape, by first dissolving the boiled egg whites overnight in a urea chemical solution. He then placed the mixture into the vortex fluid device, subjecting the whites to a high-speed five-minute spin. As the proteins brushed against the test tube walls, the force generated was enough to pull the proteins.

The result was a clear solution that looked just like diluted egg whites. At a molecular level, researchers looked at the protein lysozyme. The process of diluting the egg whites and putting them in the machine restored lysozyme back to about 85 percent of pre-boiled activity.

Read the full article on the Washington Post website