Foldit Puzzles

1528: Unsolved De-novo Freestyle 132

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!

1527: Symmetric Dimer Design: Hydrogen Bond Networks

This symmetric design puzzle has C2 symmetry, with two symmetric chains. The H-bond Network Filter encourages players to bury satisfied H-bond networks at the interface between the two chains. We've doubled the H-bond network bonus, but we'd like players to focus on building networks deep in the core of the protein complex. There a couple 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!

1526: Revisiting Puzzle 67: Integrase

This is a throwback puzzle to the early days of Foldit. This DNA-binding domain is part of a bacterial integrase protein, which facilitates the insertion of new DNA into the bacterial chromosome. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1525: Unsolved De-novo Freestyle 131

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!

1524: Symmetric Dimer Design: Hydrogen Bond Networks

This symmetric design puzzle has C2 symmetry, with two symmetric chains. The H-bond Network Filter encourages players to bury satisfied H-bond networks at the interface between the two chains. There a couple 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!

1523: Revisiting Puzzle 66: Cytochrome

This is a throwback puzzle to the early days of Foldit. This protein helps to transfer electrons between substrates in bacteria. The protein is modeled here in reducing conditions, and 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.

1522: Unsolved De-novo Freestyle 130

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!

1521: Symmetric Dimer Design: Hydrogen Bond Networks

This symmetric design puzzle has C2 symmetry, with two symmetric chains. The H-bond Network Filter encourages players to bury satisfied H-bond networks at the interface between the two chains. There a couple 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!

1520: Revisiting Puzzle 64: Thioredoxin

This is a throwback puzzle to the early days of Foldit. This human protein helps to regulate the reduction potential of the cell, and should be modeled here in reduced form (with no disulfide bonds). We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1519: HIV Protease Inhibitor Small Molecule Design: Round 2

Note: Due to player reports of persistent crashing, this puzzle is now worth zero points, so players may skip this puzzle without any effect on their rankings. However, if players would like to continue playing the puzzle, we will still analyze the puzzle solutions. And of course, we appreciate all of the detailed feedback about the puzzle!