Foldit Puzzles

1403: Revisiting Puzzle 126: Ethanolamine Utilization

This is a throwback puzzle to the early days of Foldit. This protein allows bacteria to metabolize ethanolamine and use it in constructing cell walls and cell membranes. The protein is modeled here in reduced form, 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.

1402: Unsolved De-novo Freestyle 110

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!

1401: Small Monomer Design: Larger Core

This puzzle challenges players to design a single-chain protein with 65-75 residues. The Core Existence filter has been escalated so that 35% of residues need to be buried in the protein core. The starting structure has 65 residues, but more can be added at a cost of 23 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!

1400: Revisiting Puzzle 125: Ice Binding Protein

This is a throwback puzzle to the early days of Foldit. This protein is found in cold water fishes; it binds and prevents the growth of ice crystals. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1399: Unsolved De-novo Freestyle 109

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!

1398: Extra Large Monomer Design: Smaller Core

This puzzle challenges players to design a single-chain protein with 95-120 residues. The Core Existence filter has been relaxed such that only 25% of residues need to be buried in the protein core. The starting structure has 95 residues, but more can be added at a cost of 23 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!

1397: Revisiting Puzzle 124: PDZ Domain

This is a throwback puzzle to the early days of Foldit. This domain is a component of many proteins involved in cell signaling. The protein is modeled here in reduced form, 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.

1396: Unsolved De-novo Freestyle 108

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!

1395: Medium Monomer Design: Smaller Core

This puzzle challenges players to design a single-chain protein with 75-90 residues. The Core Existence filter has been relaxed such that only 25% of residues need to be buried in the protein core. The starting structure has 75 residues, but more can be added at a cost of 23 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!

1394: Revisiting Puzzle 117: Transport Mutant

This is a throwback puzzle to the early days of Foldit. This small protein participates in electron transfer reactions in the cell. The protein is modeled here in reduced form, 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.