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This puzzle is a little different from other H-bond network design puzzles in Foldit. This protein is another dimer (i.e. two chains fold up and bind each other) that was designed in the Baker Lab. The original design has three different H-bond networks that span the interface between the two chains, but we've mutated the network residues to alanine. In order to solve this puzzle, Foldit players will have to mutate the alanine residues back into residues that can form satisfied H-bond networks. The protein backbone is fixed in this puzzle, and only the alanine residues can be mutated. We want to know how well Foldit players are able to find networks using the tools currently in Foldit.

This puzzle challenges players to design a single-chain protein with 95-120 residues. The starting structure has 95 residues, but more can be added at a cost of 32 points per residue. We've recently amended the old system of Conditions, or Filters. These have been rebranded as Objectives, and are reformulated so that they typically increase the base Foldit score (although it is still possible to receive a penalty from an Objective, in some cases). Ultimately, the function of each Objective is the same as it always has been (e.g. adding a residue still subtracts 32 points from the Residue Count objective), but we hope that the Objectives will be more encouraging than the old Filters—especially for new players who are still getting the hang of things. 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 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 C2 symmetry, with two symmetric chains. The H-bond Network Bonus encourages players to bury satisfied H-bond networks at the interface between the two chains. We've doubled the H-bond network bonus, but we'd like players to focus on building networks deep in the core of the protein complex. There are a couple other bonuses in effect; see the puzzle comments for 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 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 32 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 small peptide was discovered in platypus venom—a rare instance of mammalian-produced venom, although this peptide appears similar to more widespread antimicrobials. 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.

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 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 32 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 domain is a component of a large glycoprotein in humans that has been linked to autosomal dominant polycystic kidney disease. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

This is a followup to Puzzle 1552, where we challenged players to find two H-bond networks, starting from two extended chains. In this puzzle, both chains are already folded at the start, but players will still need to dock the two chains together and arrange the interface to find the H-bond networks. This protein is a dimer (i.e. two chains fold up and bind each other) that was designed in the Baker Lab, with two identical H-bond networks that span the interface between the two chains. See if you can find the H-bond networks!