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 1420, 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 1420 and use them as a starting point here.
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Redesign the loops of this protein to better bind the ligand! Nicotinamide mononucleotide (NMN) is a small-molecule that makes up part of the small-molecule nicotinamide adenine dinucleotide (NAD), which is sometimes regarded as 'the molecule of youth.' Scientists know that the amount of NAD in our cells declines as we age, and so designing a protein to bind to NMN is the first step towards achieving protein-based biosensors that can detect NMN levels in cells. Such biosensors would help scientists to understand the aging process and could potentially lead to a 'cure' for aging!
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This is a throwback puzzle to the early days of Foldit. Ubiquitin is a well-known protein that helps to regulate the natural turnover of proteins in the cell, and this starting structure is a model of the protein produced by Rosetta. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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Note: Due to scoreboard instabilities, the deadline for this puzzle has been extended 24 hours, to August 30 at 23:00 UTC.
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This puzzle challenges players to design a single-chain protein with 75-90 residues. We've adjusted the scoring function here so that alanine residues are more tolerable in loops (they are still restricted in helices and sheets!). The starting structure has 75 residues, but more can be added at a cost of 23 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!
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This is a throwback puzzle to the early days of Foldit. This is a throwback puzzle to the early days of Foldit. This protein helps to regulate the human immune response, and the starting structure is a Rosetta model. The protein is modeled here in the reduced state, 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.
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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!
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This puzzle challenges players to design a single-chain protein with 85-105 residues. We've adjusted the scoring function here so that alanine residues are more tolerable in loops (they are still restricted in helices and sheets!). The starting structure has 85 residues, but more can be added at a cost of 23 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!
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This is a throwback puzzle to the early days of Foldit. This small protein, from the venom of the saw-scaled viper, interferes with the cellular adhesion machinery that allows blood clotting. 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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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!