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This is a throwback puzzle to the early days of Foldit. This protein binds copper ions so that they may be transported safely to the cell compartments and enzymes that require them. 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.

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 follow-up to Puzzle 1751: De-novo Freestyle 156, now with C3 symmetry. This protein was originally designed by a Foldit player as a symmetric dimer trimer. In Puzzle 1751, 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 C3 symmetry. Players may load in solutions from Puzzle 1751. 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 storage protein is used to stockpile amino acids for future use, and is found at high concentration in the seeds of certain plants. This particular protein was used by scientists in 2011 to collect the highest-resolution crystal structure to date. This protein 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.

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!

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 eelpout protein binds nucleated ice crystals to inhibit their growth. 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 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!

Design a protein that binds IL-7R!

Design a protein that binds IL-7R!