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This is a follow-up to Puzzle 1634: De-novo Freestyle 146,now with C2 symmetry. This protein was originally designed by a Foldit player as a symmetric dimer. In Puzzle 1634, 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 1634. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!

This is a throwback puzzle to the early days of Foldit. This protein is found in the nucleus of stem cells in mice, and is important for maintaining the pluripotency of the stem cell. 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.

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 50 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!

This is a follow-up to Puzzle 1637, now with C2 symmetry. This protein was originally designed as a symmetric dimer, and we want to see if Foldit players can predict how the symmetric protein was designed to fold and bind. Players may load in solutions from Puzzle 1637. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!

This is a throwback puzzle to the early days of Foldit. This is a portion of a troponin protein found in the skeletal muscle of turkeys. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

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). No more than 50% of residues may form 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!

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!

This is a throwback puzzle to the early days of Foldit. This is a trypsin inhibitor in pumpkins. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been. Players will NOT be able to load in any previous solutions for these puzzles.

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). No more than 50% of residues may form 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!

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!