Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
-
This is a throwback puzzle to the early days of Foldit. This is a throwback puzzle to the early days of Foldit. This protein helps to regulate the human immune response, and the starting structure is a Rosetta model. The protein is modeled here in the reduced state, so no disulfides are expected to form. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
-
This symmetric design puzzle has C4 symmetry, with four symmetric chains. The Hbond Network Filter encourages players to bury satisfied Hbond networks at the interface, but note that no more than six inter-molecular Hbonds may contribute to the filter! There are several other filters 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!
-
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!
-
This is a throwback puzzle to the early days of Foldit. This small protein, from the venom of the saw-scaled viper, interferes with the cellular adhesion machinery that allows blood clotting. This protein contains eight cysteine residues 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.
-
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!
-
This symmetric design puzzle has C3 symmetry, with three symmetric chains. The Hbond Network Filter encourages players to bury satisfied Hbond networks at the interface, but note that no more than six inter-molecular Hbonds may contribute to the filter! There are several other filters 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!
-
This is a throwback puzzle to the early days of Foldit. This protein comes from the bacteria Escherichia coli, but its function is still unknown! We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
-
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!
-
This puzzle has two 55 residue chains, but they are not symmetric; you have 110 independent residues to work with! The Hbond Network Filter encourages players to bury satisfied Hbond networks at the dimer interface, but note that no more than four inter-molecular Hbonds may contribute to the filter! There are several other filters 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!
-
This is a throwback puzzle to the early days of Foldit. This protein shuttles lipids between cell membranes in the rice plant. The 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.