puzzle picture
1905: Aflatoxin Challenge: Round 19 Loop Prediction
Status: Closed

Summary

Name: 1905: Aflatoxin Challenge: Round 19 Loop Prediction
Status: Closed
Created: 10/16/2020
Points: 100
Expired: 10/23/2020 - 18:00
Difficulty: Novice
Description: Refold the loops in this Aflatoxin Challenge design! In the most recent lab tests the Siegel Lab identified three well-behaved designs that show activity against aflatoxin. We want to know how these designs fold in the absence of aflatoxin. This puzzle features a protein designed by Phyx in Puzzle 1739, but the starting structure has been partially unfolded. Help us predict the structure of this design by folding the redesigned loops!

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 19th 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: Overall, Prediction

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RankGroupScorePoints
1L'Alliance Francophone9,720100
2Beta Folders9,70074
3Go Science9,59754
4Anthropic Dreams9,56938
5Gargleblasters9,49727

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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, RosettaCommons