Foldit Puzzles

1679: Unsolved De-novo Freestyle 153

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!

1678: Extra Large Monomer Design

This puzzle challenges players to design a single-chain protein with 95-120 residues. The starting structure has 95 residues, but more can be added at a cost of 55 points per residue. See the puzzle comments for Objective 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!

1677: Revisiting Puzzle 137: Rosetta Decoy

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.

1676: Unsolved De-novo Freestyle 152: Symmetric Dimer

This is a follow-up to Puzzle 1673: De-novo Freestyle 152, now with C2 symmetry. This protein was originally designed by a Foldit player as a symmetric dimer. In Puzzle 1673, we challenged the Foldit community to try and predict how the design might fold as a single, monomeric chain. Now we want to see if Foldit players can predict how the original protein was designed to fold and bind to itself with C2 symmetry. Players may load in solutions from Puzzle 1673. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!

1675: Integrin Antagonist Binder Design: Round 3

Help design a protein binder for cancer therapy!

1674: Revisiting Puzzle 136: Cell Adhesion

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.

1673: Unsolved De-novo Freestyle 152

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!

1672: Large Monomer Design

This puzzle challenges players to design a single-chain protein with 85-105 residues. The starting structure has 85 residues, but more can be added at a cost of 55 points per residue. See the puzzle comments for Objective 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!

1671: Revisiting Puzzle 135: E. coli

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.

1670: Unsolved De-novo Freestyle 150: Symmetric Dimer

This is a follow-up to Puzzle 1657: De-novo Freestyle 150, now with C2 symmetry. This protein was originally designed by a Foldit player as a symmetric dimer. In Puzzle 1657, we challenged the Foldit community to try and predict how the design might fold as a single, monomeric chain. Now we want to see if Foldit players can predict how the original protein was designed to fold and bind to itself with C2 symmetry. Players may load in solutions from Puzzle 1657. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!