Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
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This is a throwback puzzle to the early days of Foldit. This small toxin is produced from the funnel-web spider A. aperta, and induces paralysis in insects by blocking calcium channels. This protein contains eight cysteines that oxidize to form four disulfide bonds. 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 an error that prevented players from opening the puzzle. The puzzle has been reposted as Puzzle 1619b.
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This symmetric design puzzle has C3 symmetry, with three symmetric chains. The H-bond Network Objective encourages players to bury H-bond Networks at the interface between the two chains. We've doubled the H-bond Network bonus, but we'd like players to focus on building networks deep in the core of the protein complex. There are a couple other bonuses in effect; see the puzzle comments for 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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The structure of this protein is still unknown. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!
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This is a throwback puzzle to the early days of Foldit. In the struggle for limited resources, some strains of the bacteria E. coli produce a potent toxin to fight off competing strains. This small immunity protein protects the aggressor E. coli from falling victim to its own toxin. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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This symmetric design puzzle has C3 symmetry, with three symmetric chains. The H-bond Network Objective encourages players to bury H-bond Networks at the interface between the two chains. We've doubled the H-bond Network bonus, but we'd like players to focus on building networks deep in the core of the protein complex. There are a couple other bonuses in effect; see the puzzle comments for 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 was posted erroneously with the wrong setup. The puzzle was closed early, and has been reposted with the correct setup as Puzzle 1615b.
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The structure of this protein is still unknown. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!
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This is a throwback puzzle to the early days of Foldit. This protein is found on the surface of bacteriophage fd, a virus that infects E. coli. It is responsible for penetrating the cell membrane of the host bacteria, allowing virus to enter the cell. This protein contains four cysteines that oxidize to form two disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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This symmetric design puzzle has C2 symmetry, with two symmetric chains. The H-bond Network Objective encourages players to bury H-bond Networks at the interface between the two chains. We've doubled the H-bond Network bonus, but we'd like players to focus on building networks deep in the core of the protein complex. There are a couple other bonuses in effect; see the puzzle comments for 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!