Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
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This is a follow-up puzzle for Puzzle 1120, now with Predicted Contacts to help guide your folding! See the blog for information on using the contact map. You can see the predicted contacts for this protein by clicking the Contact Map button in the Main menu (Selection Interface) or in the Actions tab (Classic Interface). You will notice that different contacts are shown in different shades of green, with brighter green contacts indicating stronger predictions. Players will be able to load in manual saves from Puzzle 1120 and use them as a starting point here.
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This is a slight variant on the last 17-residue Marburg design puzzle. Based on the results from that puzzle, we've changed the following:
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This is a slight variant on the last 17-residue Marburg design puzzle. Based on the results from that puzzle, we've changed the following:
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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'd like to model 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.
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The structure of this protein is still unsolved. The PSIPRED secondary structure predictions are provided on the starting model.
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This is a throwback puzzle to the early days of Foldit. This toxin, which is released by the sea anemone A. xanthogrammica, disrupts normal contraction of cardiac muscle in potential predators, and furthermore serves as a pheromone to signal danger to nearby anemones. 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.
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This puzzle is very similar to Puzzle 1115, though the HBNet filter has been slightly tweaked. In this puzzle, the bonus for H-bond networks has been doubled, but only Hbond networks that are at least 75% satisfied will be rewarded. There are several other filters 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!
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This is the third in our series of Marburg inhibitor peptide puzzles. We'd like you to design a 17-residue peptide that's able to inhibit the Marburg glycoprotein, a viral surface protein that allows the Marburg virus to infect cells. Seventeen residues might seem quite small, but smaller size can make it easier for a peptide to pass through barriers, such as the gut-blood barrier or the blood-brain barrier, and can also make it less likely to trigger an immune response. It's also quite easy to synthesize a peptide this small, which can mean both that we can make large amounts and that we can include unnatural amino acids or other chemical modifications that would not be possible in a protein that's expressed in bacteria or yeast, but which might aid function or stability. The flip side, though, is that it's more challenging to design something that folds well and binds with high affinity and specificity in this small size range -- but that's the challenge!
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This is a throwback puzzle to the early days of Foldit. This toxin, produced by the Chinese cobra N. atra, induces contracture in skeletal and cardiac muscle. This protein contains eight cysteine residues 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.
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This puzzle combines the new HBNet filter with full-blown symmetric design. There are several other filters 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!