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1806: Aflatoxin Challenge: Round 15 Loop Prediction
Status: Closed


Name: 1806: Aflatoxin Challenge: Round 15 Loop Prediction
Status: Closed
Created: 02/28/2020
Points: 100
Expired: 03/06/2020 - 23:00
Difficulty: Intermediate
Description: Refold the loops in this Aflatoxin Challenge design! This puzzle is similar to Puzzle 1803, but the starting structure comes from a different Foldit player design. After Round 13 of the Aflatoxin Challenge, where Foldit players redesigned the binding loops of an oxidation enzyme, the Siegel Lab found that some designs had high oxidative activity for other molecules--but no activity against aflatoxin! We think the redesigned loops might be misfolding when aflatoxin is not in the binding pocket. Misfolded loops could prevent the enzyme from binding aflatoxin and catalyzing the oxidation reaction. We wonder if Foldit players can predict how these binding loops might misfold, by refolding the loops in ways that score better than the original design! If we can figure out how the binding loops misfold, then we might be able to fix them and recover activity against aflatoxin!

Aflatoxins are a class of poisonous compounds that contaminate a significant portion of the global food supply. In the most recent phase of Foldit's Aflatoxin Challenge, the Siegel Lab at UC Davis proposed a new strategy for degrading aflatoxin, asking Foldit players to help redesign an oxidation enzyme so that it could break down aflatoxin molecules. In this puzzle, players can refold the two binding loops of the redesigned enzyme. The rest of the protein is frozen, except for some sidechains that might interact with the binding loops. No mutations or insertions are allowed. Since we are interested in how the protein might fold without aflatoxin, there is no aflatoxin molecule in the binding pocket.

This is the 15th round of our Aflatoxin Challenge, sponsored by Mars Inc. and Thermo Fisher Scientific. Promising designs will be tested by the Siegel Lab at UC Davis. By participating in the challenge/game, the players agree that all player designs will be available permanently in the public domain, and the players will not seek intellectual property protection over the designs created as part of the challenge/game.
Categories: Design, Overall

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Developed by: UW Center for Game Science, UW Institute for Protein Design, Northeastern University, Vanderbilt University Meiler Lab, UC Davis
Supported by: DARPA, NSF, NIH, HHMI, Amazon, Microsoft, Adobe, Boehringer Ingelheim, RosettaCommons