Foldit Puzzles

1603: Unsolved De-novo Freestyle 138

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!

1602: Symmetric Dimer Design

This symmetric design puzzle has C2 symmetry, with two symmetric chains. There is no H-bond Network Objective in this puzzle, so the interface can be completely nonpolar (orange sidechains). However, there other stringent objectives in effect: solutions may have no more than 50% of residues in helices, and all loops must match one of the Ideal Loop Building Blocks found in the Blueprint tool. 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!

1601: Revisiting Puzzle 87: Zinc Binding Protein

This is a throwback puzzle to the early days of Foldit. This small peptide is part of a larger protein that helps to regulate cell division, and is very important in early embryonic development. The protein is modeled here as in a reduced environment, so no disulfide bonds are expected to form. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1598: Cryo-EM Freestyle with Density

This protein is another part of the same protein complex with multiple subunits from Puzzle 1554 and Puzzle 1588, which has been the target of cryo-EM experiments. We are giving you an extended chain to start with, so good luck!

1600: Symmetric Dimer Design

This symmetric design puzzle has C2 symmetry, with two symmetric chains. There is no H-bond Network Objective in this puzzle, so the interface can be completely nonpolar (orange sidechains). However, solutions may have no more than 50% of residues in helices. 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!

1597: Aflatoxin Challenge: Round 12b

Note: This puzzle is much like Puzzle 1595, which had problems with shared solutions. Unfortunately, players will not be able to load in solutions from Puzzle 1595 or previous rounds of the Aflatoxin Challenge.

1599: Revisiting Puzzle 86: Nematode

This is a throwback puzzle to the early days of Foldit. This protein, isolated from the hookworm A. caninum, is an extremely potent anticoagulant. This protein contains ten cysteine residues that oxidize to form five disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1596: Revisiting Puzzle 85: Cell Adhesion Protein

This is a throwback puzzle to the early days of Foldit. This small domain is part of a larger protein that mediates interactions between other proteins in human development. This protein contains several cysteine residues, but we are modeling them in a reducing environment, so they should NOT form disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1595: Aflatoxin Challenge: Round 12

Note: Due to a bug in solution sharing and loading, this puzzle is worth zero points and will close early. We encourage players to play replacement puzzle Puzzle 1597 instead, although we will still analyze the solutions from this puzzle if players wish to keep working on their designs. Unfortunately players may not load solutions from this puzzle into the replacement Puzzle 1597.