It’s not every day that we log into Facebook and Twitter to see conversations about denaturing proteins and the possibility of reducing biotechnology costs, but that changed last week when a story about “unboiling” eggs became a trending topic.
Since NIGMS partially funded the research advance 
that led to the media scramble, we asked our scientific expert Jean Chin to tell us more about it.
What’s the advance?
Gregory Weiss of the University of California, Irvine, and his collaborators have designed a device that basically unties proteins that have been tangled together.
Why’s this important?
Many human proteins or their cousins from other mammals can be made in bacterial cells. These cells can quickly produce the large quantity of a protein that researchers need to study its structure, function, dynamics and potential clinical value. But there’s a catch: The proteins can end up in clumps stored inside structures called inclusion bodies. The current methods to release and refold the proteins take days and are expensive.
This new device can do it quickly—in just minutes—and cheaply, saving researchers, pharmaceutical companies and others interested in making useful proteins time and money.
What’s the egg connection?
One of the proteins used to test the device is lysozyme, which makes up about 4 percent of the protein content of egg white. The researchers boiled egg white lysozyme and used the device to refold the protein back into its normal form.
Unboiling an egg was a great hook to get people’s attention, but the real goal of the work is to unfold and refold proteins for biomedical research and biotechnology applications.
This work was funded in part by NIH under grant R01GM100700.