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Puzzle
Expired: 02/08/18 23:00:00
Top Group: Void Crushers
Top Player: JSmith48
Top Score: 8,694
Categories: Beginner
This small unsolved Arabidopsis protein only has 59 residues and negatively controls the biosynthesis of starch in plants and regulates leaf and seed composition. We are giving you 5 starts for this puzzle. Resetting the puzzle will cycle through these 5 Zhang server predictions. They are also in the Alignment Tool so you can use partial threading as well as an extended chain. For players with fewer than 150 global points.
Puzzle
Expired: 01/05/18 23:00:00
1 comment
Top Group: Gargleblasters
Top Player: Skippysk8s
Top Score: 10,511
Categories: Design, Overall
This puzzle challenges players to design a single-chain protein with 75-90 residues. We've softened the penalties associated with the Core Existence filter, which have typically been very steep. The starting structure has 75 residues, but more can be added at a cost of 16 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!
Puzzle
Expired: 01/03/18 18:00:00
3 comments
Top Group: Go Science
Top Player: toshiue
Top Score: 8,310
Categories: Pilot
In this Classroom puzzle, students will learn about RNA structure and dynamics, as well as the ongoing debate between conformational capture and induced fit models of biomolecular binding. The RNA molecule of choice here, HIV TAR, is provided in one of its many possible folded conformations. However, we know the RNA is flexible, and it is still unclear what fold is most favorable for this molecule. See if you can find other stable folds for this RNA molecule!
Puzzle
Expired: 01/04/18 23:00:00
5 comments
Top Group: Gargleblasters
Top Player: Blipperman
Top Score: 10,183
Categories: Overall, Prediction
This protein is a component of reindeer milk. Beta-lactoglobulin is a protein found in the milk of many mammals, including cows and sheep, but not in humans. Its natural function is still unknown. The structure of this protein was determined (with some difficulty) by x-ray crystallography in 2006. However, parts of the published structure are a little bit problematic. We want to see if Foldit players can fold this protein starting from an extended chain. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets! Note that, due to the large size of the protein, this puzzle will be active for two weeks.
Puzzle
Expired: 02/01/18 23:00:00
Top Group: Void Crushers
Top Player: Madde
Top Score: 11,007
Categories: Beginner
This is a small symmetric trimer design puzzle. A symmetric protein relies not only on how well folded each part is, but also on how well they interface together. Your changes will be reflected in the symmetric unit. Make sure you have completed Intro Puzzle 5-2, and 7-1 through 7-4. For players with fewer than 150 global points.
Puzzle
Expired: 12/26/17 18:00:00
2 comments
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 8,927
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This enzyme helps to regenerate a cofactor that is necessary for nucleic acid synthesis; the starting structure is a model produced by Rosetta. This protein contains only one cysteine, so no disulfide bonds are expected. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
Puzzle
Expired: 12/28/17 23:00:00
4 comments
Top Group: Gargleblasters
Top Player: Skippysk8s
Top Score: 10,821
Categories: Design, Overall
This puzzle challenges players to design a single-chain protein with 85-105 residues. We've softened the penalties associated with the Core Existence filter, which have typically been very steep. The starting structure has 85 residues, but more can be added at a cost of 16 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!
Puzzle
Expired: 01/25/18 23:00:00
Top Group: Anthropic Dreams
Top Player: JSmith48
Top Score: 8,932
Categories: Beginner
We are giving you a helix positioned over a hydrophobic groove where binding occurs in nature. You can mutate any residue on the helix but none on the native binding region. Try to look for favorable hydrophobic interactions in this groove while maintaining the helix. For players with fewer than 150 global points.
Puzzle
Expired: 12/19/17 18:00:00
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 10,247
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This protein was evolved in vitro to bind testosterone; the starting structure is a model produced by Rosetta. This protein contains two cysteine residues, which oxidize to form a single disulfide bond. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
Puzzle
Expired: 12/18/17 23:00:00
1 comment
Top Group: Beta Folders
Top Player: smilingone
Top Score: 10,212
Categories: Design, Overall
This puzzle challenges players to design a single-chain protein with 65-75 residues. We've softened the penalties associated with the Core Existence filter, which have typically been very steep. The starting structure has 65 residues, but more can be added at a cost of 16 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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Developed by: UW Center for Game Science, UW Institute for Protein Design, Northeastern University, Vanderbilt University Meiler Lab, UC Davis
Supported by: DARPA, NSF, NIH, HHMI, Amazon, Microsoft, Adobe, RosettaCommons