Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
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This spinach protein is critical for photosynthesis, and participates in the electron transfer chain within the chloroplast. The protein is modeled here in the reduced state, so no disulfides are expected to form. In this experimental puzzle you will have 128 moves at your disposal. Once you use them up, you can reset and try something else!
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This puzzle challenges players to design a single-chain protein with 95-120 residues. The starting structure has 95 residues, but more can be added at a cost of 32 points per residue. See the puzzle comments for filter details. The Baker Lab will run folding predictions on your solutions for this puzzle, and those that perform well will be synthesized in the lab. Remember, you can use the Upload for Scientists button for up to 5 designs that you want us to look at, even if they are not the best-scoring solutions!
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This protein has 92 residues! It was designed by the Baker Lab in 2003, and has a topology unlike any natural protein yet discovered. In this experimental puzzle you will have 256 moves at your disposal. Once you use them up, you can reset and try something else!
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These are the two chains of a bio-engineered variant of human insulin, which contains six cysteine residues that oxidize to form three disulfide bonds. In this experimental puzzle you will have 128 moves at your disposal. Once you use them up, you can reset and try something else!
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This puzzle challenges players to design a single-chain protein with 75-90 residues. The starting structure has 75 residues, but more can be added at a cost of 32 points per residue. See the puzzle comments for filter details. The Baker Lab will run folding predictions on your solutions for this puzzle, and those that perform well will be synthesized in the lab. Remember, you can use the Upload for Scientists button for up to 5 designs that you want us to look at, even if they are not the best-scoring solutions!
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Note: This puzzle replaces Puzzle 1542 which was closed early due to a bug.
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This is a throwback puzzle to the early days of Foldit. This short protein is a component of the α-ketoglutarate dehydrogenase complex, which is best known for its role in the citric acid cycle. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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Note: This puzzle was closed early due to a missing filter file resulting in no bonuses being received for forming disulfide bonds. It is superseded by Puzzle 1542b. Players may load their work from this puzzle into the reposted puzzle.
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Redesign the active site to bind aflatoxin! This puzzle is much like Round 7 of the Aflatoxin Challenge, but now the aflatoxin molecule is no longer frozen, and can be moved within the active site. 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. Although no extra residues may be inserted in this puzzle, players may remove residues at positions 62-67, which clash with the aflatoxin molecule. 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.
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This puzzle challenges players to design a single-chain protein with 85-105 residues. The starting structure has 85 residues, but more can be added at a cost of 32 points per residue. See the puzzle comments for filter details. The Baker Lab will run folding predictions on your solutions for this puzzle, and those that perform well will be synthesized in the lab. Remember, you can use the Upload for Scientists button for up to 5 designs that you want us to look at, even if they are not the best-scoring solutions!