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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 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!

This is a throwback puzzle to the early days of Foldit. This protein comes from the bacteria Escherichia coli, but its function is still unknown! We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

This is a follow-up to Puzzle 1657: De-novo Freestyle 150, now with C2 symmetry. This protein was originally designed by a Foldit player as a symmetric dimer. In Puzzle 1657, 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 1657. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!

This puzzle challenges players to design a single-chain protein with 60-65 residues. The starting structure has 60 residues, but more can be inserted at a cost of 55 points per residue. See the puzzle comments for filter 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 shuttles lipids between cell membranes in the rice plant. The protein contains eight cysteines that oxidize to form four disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

This Electron Density puzzle is different than anything we've ever posted before! The extended chain is 187 residues long, but we are giving you a lot more density than that. You'll need to find where to fit this chain in the giant blob of density. (The "Trim Density" tool will be your friend)

This is a throwback puzzle to the early days of Foldit. This protein allows bacteria to metabolize ethanolamine and use it in constructing cell walls and cell membranes. The protein is modeled here in reduced form, 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 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!

Help design a protein binder for cancer therapy!

This is a throwback puzzle to the early days of Foldit. This protein is found in cold water fishes; it binds and prevents the growth of ice crystals. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.