Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
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This puzzle has been reposted. Please use the new version of this puzzle, 688b. You may load your MANUAL saves into the new puzzle.
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This is the sequel to puzzle 675, where you folded two symmetric chains attached to a central catalyst molecule. We've kept the catalyst and the chains identical, but we're moving beyond just folding: it's time to make this catalyst go turbo. It needs protons fed to its inner nitrogen (an H-bond acceptor) to go faster, so we're giving you a large bonus for making an H-bond to this atom. Fair warning: it's a bit crowded in there, so the angle has to be just-right to avoid a clash.
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This currently unsolved short protein does not have any templates that we can use, so we are giving it to you as an extended chain. Use all your skills to fold it up as best as you can. The secondary structure predictions are provided on the starting model, with more details posted in the puzzle comments.
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We are giving you a single chain of 76 residues to design. You will need the latest version of the client to play this puzzle
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We are giving you a Foldit prediction by wudoo from Puzzle 671 for you to refine. Only GUI scripts are allowed and sharing has been disabled. After this puzzle expires, the puzzle will be re-posted and LUA scripts and sharing will be allowed. You'll be able to load in your solutions from this puzzle and use scripting and sharing.
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This is round 2 for Puzzle 680. You will be able to load in your manual saves from 680 and use them as a starting point here. This puzzle has been opened up to allow for sharing and the use of all scripts. See if you can improve your model from the first round using these tools, or start from scratch! NOTE: If you did not manually save a solution in puzzle 680, you can go back to 680, manually save it, and the solution should appear in your manual saves for this puzzle.
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We are giving you a symmetric trimer of 40 residues to design. Remember, a symmetric protein relies not only on how well folded each part is, but also on how well they interface together - and a symmetric trimer can be thought of as having three 2-fold interfaces.
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We are reposting this 33 residue CASP10 target to try out the new
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In this puzzle, we've taken the results from a previous puzzle (Blind Electron Density 5), and used the top player solutions to refine the density! Your fellow folders' efforts have made the density clearer and easier to work with. The same rules apply - find the best fold that fits the protein into the density in order to maximize your score!
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Sugar molecules such as the one here are coated on the surface of many human pathogens. We are attempting to increase the protein-sugar binding interactions by allowing you to redesign & insert up to 10 residues to form additional hydrogen bonds with the sugar. To encourage this, only GUI scripts are allowed, and sharing has been disabled. After this puzzle expires, the puzzle will be re-posted and LUA scripts and sharing will be allowed. You will be able to load in your solutions from the first puzzle and refine them with scripting and sharing. Please read the new blogpost & puzzle comments for more details.