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This is a throwback puzzle to the early days of Foldit. This protein was designed by the Baker Lab in 2003, and has a topology unlike any natural protein yet discovered. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

Design a protein for electron transfer! See the blog for more details!

This symmetric design puzzle has C3 symmetry, with three symmetric chains. This puzzle is a little different from other symmetry puzzles, in that we want players to focus on building a smaller interface between the chains. The "Core Limit: Complex" objective will incur penalties if there are too many buried residues in the total assembly. 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 throwback puzzle to the early days of Foldit. This protein binds fatty acids in intestinal cells. 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 75-90 residues. The starting structure has 75 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!

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 small, intracellular domain binds to the CD2 T cell receptor (TCR), and plays a critical role in T cell activation during the immune response. 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. 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. We've omitted the "Core Exists: Complex" objective to simplify the puzzle, but we still expect that designs with a strong hydrophobic interface (orange sidechains) will score best. 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 1691: De-novo Freestyle 154, now with C2 symmetry. This protein was originally designed in the Baker Lab to bind to a different protein, but some lab results suggests the protein binds to itself as a dimer. In Puzzle 1691, 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 protein might fold and bind to itself with C2 symmetry. Players may load in solutions from Puzzle 1691. 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. These are the two chains of a bio-engineered variant of human insulin, which contains six cysteine residues that oxidize to form three disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.