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This is a throwback puzzle to the early days of Foldit. This protein is secreted at the site of inflammation, recruiting monocytes and T cells to help fight an infection. This protein contains four cysteine residues that oxidize to form two disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

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 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!

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.

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!

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.

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!

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.

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.

The goal of this puzzle is to change the chemical structure of the ligand in the center of the protein to find better inhibitors of HIV protease. It's less about changing the protein to fit the ligand, and more about changing the ligand to fit the protein. Use the Ligand Design tool in the selection interface (or the "Ligand Design" mode in the original interface) to alter the chemical identity of the inhibitor.