Foldit Puzzles

1221: Disordered Electron Density: Round 1

NOTE: Because many players have had trouble playing this puzzle, the puzzle has been made worth zero points, and it will not contribute to player rankings. However, this puzzle is still of unique scientific interest, and we encourage players to work on it if they are able!

1220: 70 Residue Monomer Design: Residue Count Filter

This design puzzle features a new filter: the Residue Count filter incurs a penalty when a player inserts extra residues beyond the 70 residue limit. The filter is intended to give players the flexibility to temporarily add residues to a design-in-progress. 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!

1219: Revisiting Puzzle 147: Rosetta Decoy 10

This is a throwback puzzle to the early days of Foldit. This protein is part of a signaling pathway that regulates sporulation in B. subtilis; the starting structure is a model produced by Rosetta. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1218: Unsolved De-novo Freestyle 77

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!

1217: 80 Residue Monomer Design: Residue Count Filter

This design puzzle features a new filter: the Residue Count filter incurs a penalty when a player inserts extra residues beyond the 80 residue limit. The filter is intended to give players the flexibility to temporarily add residues to a design-in-progress. 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!

1216: Revisiting Puzzle 146: Rosetta Decoy 9

This is a throwback puzzle to the early days of Foldit. This protein is a phosphatase that participates in several metabolic pathways; the starting structure is a model produced by Rosetta. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1215b: Unsolved De-novo Freestyle 76

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!

1215: Unsolved De-novo Freestyle 76

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!

1214: 65 Residue Monomer Design: Residue Count Filter

This design puzzle features a new filter: the Residue Count filter incurs a penalty when a player inserts extra residues beyond the 65 residue limit. The filter is intended to give players the flexibility to temporarily add residues to a design-in-progress. 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!

1213: Revisiting Puzzle 144: Rosetta Decoy 8

This is a throwback puzzle to the early days of Foldit. The function of this thermophilic protein is unknown, but it is unusual among intracellular proteins in that the native structure includes disulfide bonds. This protein contains six cysteine residues that are oxidized to form three disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.