The person who first discovered this “unboiling” technique was Gregory Weiss, a chemistry professor at the University of California-Irvine. Inspired by a collaborator’s use of a vortex-fluid device to pull apart other kinds of complex structures, Weiss wondered if that rotational energy could disentangle boiled egg-white proteins, too. As it turns out, it could. To read Weiss' paper, go here.

How important are proteins and protein folding? Protein folding is a complicated topic, and it has implications way beyond hard-boiled eggs. Proteins are the essential functional components of the body. The enzymes that catalyze the biochemical reactions that digest food and produce energy; the antibodies that help fight off disease; signaling molecules like insulin that carry information from one part of the body to another; molecules like hemoglobin that carry oxygen throughout the body: all of these are proteins. Pretty essential aren’t they?

The function of all these proteins depends on their ability to recognize and tightly bind to specific other substances. Like a key fitting in a lock, this only works if the protein is the right shape. If the protein is folded incorrectly, it usually won’t work properly. Incorrect protein folding can have serious consequences. Alzheimer’s Disease, Huntington’s Disease, and amyotrophic lateral sclerosis are all associated with misfolded proteins that build up in or around neurons and interfere with their function. Prion diseases like bovine spongiform encephalitis (mad cow disease) are caused by improperly-folded prion proteins that cause healthy prions to fold incorrectly, too. And if a tumor-suppressing protein called p53 gets folded improperly, it can’t keep potentially cancerous cells from proliferating. This mutation is found in about half of all cases of cancer—and for certain cancer types, it’s almost universal.

Just as incorrectly folded proteins can wreak havoc on the body, correctly folded ones can be incredibly helpful. Many highly effective medications are proteins that replace missing or misfolded ones, or even perform entirely new functions. Insulin was the first and best-known protein used as a medication. Other protein therapeutics help treat multiple sclerosis, autoimmune diseases, osteoporosis, cystic fibrosis, and a host of other conditions.

So figuring out how proteins are supposed to be folded is really important for both understanding and treating disease—but it’s also really hard, because most biological proteins are huge, complex molecules with an almost infinite number of possible configurations. There are a few methods to determine the structure of a protein by observation, but they don’t always work. Many scientists turn to computations, which can test many possible configurations to identify which one is the most stable. But this can take a long time. How has that changed recently?

Enter the online game called Foldit! To speed up the process, in 2008 scientists created a free online game called Foldit, where players can take a real protein and try to fold it into the best conformation. Hundreds of thousands of gamers all over the world can collaborate on the structure of a single protein, dramatically increasing the computing power applied to the problem. Check out the Science Behind Foldit here! What were the results? In 2011, Foldit players solved the structure of a protein that helps an AIDS-like virus replicate; a few months later, they designed a new protein that was eighteen times more active than the version scientists had originally created. Wow!

Isn’t it truly amazing what many brains working together can solve? Join in and see if you can help by participating in a little Citizen Science! Then, watch this TED Talent search talk by Zoran Popovich and learn more about ins and outs of using “Massive multiplayer games to solve complex scientific problems.” What “game” will be designed next that could solve a medical dilemma? Any ideas?

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