Crowd-sourced gamers advance AIDS research
By Ben Coxworth
September 20, 2011
It was a puzzle that had thwarted scientists for almost a decade, but a collection of gamers was able to solve it in just three weeks. What the scientists wanted to know was the structure of retroviral proteases, a class of enzymes that play a key part in the maturation and proliferation of the AIDS virus. The mystery was crowd-sourced to the gaming community within an existing online game known as Foldit, by researchers from the University of Washington. The game challenges players to collaborate and compete in predicting the structure of protein molecules.
The gamers were collectively able to create models that were close enough to the real thing, that the researchers were able to refine the results within just a few days, and arrive at their answer. Not only do they now have a much better understanding of the enzyme, but specific surface areas on the molecule look like they could be good targets for its deactivation.
Thousands of players from all over the world took part in the challenge. Gamers progressed through different skill levels, using their 3D spatial abilities to virtually rotate chains of amino acids. A molecule-assembling program named Rosetta, along with onscreen manipulation tools, helped them in their task. One of those tools allowed them to copy parts of known molecules, and see how they might fit into the incomplete model. The researchers updated the puzzle as more pieces fell into place.
Now that the retroviral protease structure is known, the development process of drugs that can stop the AIDS virus may be greatly accelerated.
"People have spatial reasoning skills, something computers are not yet good at," said U Washington's Dr. Seth Cooper, lead designer and developer of Foldit. "Games provide a framework for bringing together the strengths of computers and humans [...] Gaming, science and computation can be combined to make advances that were not possible before."
The research was recently published in the journal Nature Structural & Molecular Biology.
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