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1550: Aflatoxin Challenge: Round 10
Status: Closed


Name: 1550: Aflatoxin Challenge: Round 10
Status: Closed
Created: 07/17/2018
Points: 100
Expired: 07/31/2018 - 23:00
Difficulty: Intermediate
Description: Redesign the active site to bind aflatoxin! This puzzle is much like Round 9 of the Aflatoxin Challenge, but now players may insert up to 20 extra residues into the designable loops, at a cost of 20 points per residue. Strong constraints will keep aflatoxin from moving too far from its starting position, but we think the extra wiggle room will allow Foldit players to design an active site that binds the molecule more tightly. Parts of the scaffold protein have been trimmed to reduce the size of the puzzle, and we've upweighted ligand interactions by a factor of five. We'd like to see if Foldit players can design proteins that make more interactions with the ligand! See the blog for more details.

Aflatoxins are a class of poisonous compounds that contaminate a significant portion of the global food supply. In this puzzle, players are challenged to redesign an enzyme that could break down aflatoxin molecules. The majority of the protein is frozen, with the aflatoxin ligand fixed in a binding pocket. Surrounding the binding pocket are a number of loops that might be redesigned without affecting the folding stability of the protein. In these loops, players may manipulate the protein backbone and mutate the residue sidechains. Redesign the loops of this protein to better bind the aflatoxin ligand!

This is the tenth puzzle 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