Foldit Puzzles

1472: Unsolved De-novo Freestyle 124

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!

1471: 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.

1470: Small Monomer Design

This puzzle challenges players to design a single-chain protein with 65-75 residues. In this design puzzle, we've deactivated the Ideal Loops filter, so players have more flexibility to design their own high-scoring loops! The starting structure has 65 residues, but more can be added at a cost of 16 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!

1469: Unsolved De-novo Freestyle 123

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!

1468: 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.

1467: Extra Large Monomer Design

This puzzle challenges players to design a protein with 95-120 residues. We've softened the penalties associated with the Core Existence and Residue Count filters, which have typically been very steep. The starting structure has 95 residues, but more can be added at a cost of 16 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!

1466: Unsolved De-novo Freestyle 122

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!

1465: 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.

1464: Medium Monomer Design

This puzzle challenges players to design a single-chain protein with 75-90 residues. We've softened the penalties associated with the Core Existence filter, which have typically been very steep. The starting structure has 75 residues, but more can be added at a cost of 16 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!

1462: Reindeer Beta-lactoglobulin

This protein is a component of reindeer milk. Beta-lactoglobulin is a protein found in the milk of many mammals, including cows and sheep, but not in humans. Its natural function is still unknown. The structure of this protein was determined (with some difficulty) by x-ray crystallography in 2006. However, parts of the published structure are a little bit problematic. We want to see if Foldit players can fold this protein starting from an extended chain. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets! Note that, due to the large size of the protein, this puzzle will be active for two weeks.