puzzle picture
1510: Aflatoxin Challenge: Round 8
Status: Closed


Name: 1510: Aflatoxin Challenge: Round 8
Status: Closed
Created: 04/18/2018
Points: 100
Expired: 05/02/2018 - 23:00
Difficulty: Intermediate
Description: Redesign the active site to bind aflatoxin! This puzzle uses the same starting structure as Round 7 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. 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 eighth 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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Joined: 05/19/2009
Groups: Contenders
How is ligand scoring measured ?

"we've upweighted ligand interactions by a factor of five"
In what way are the interactions valued ? How does the scoring for these interactions take place ?
I find little score benefit from a bonding sidechain versus a non-bonding sidechain.

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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