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Puzzle
Expires: 05/04/17 18:00:00
Top Group: Gargleblasters
Top Player: frood66
Top Score: 9,913
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This saposin protein from pig serves as an activator for lipid-desolving enzymes. This protein contains six cysteines 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.
Puzzle
Expires: 06/08/17 23:00:00
Top Group: Bioquimica Biotec UFRJ 2017-1
Top Player: carsonfb
Top Score: 8,319
Categories: Beginner
We are giving you this currently unsolved short protein as an extended chain. It has only 48 residues and we're posting it with no secondary structure predictions. For players with fewer than 150 global points.
Puzzle
Expires: 05/01/17 23:00:00
1 comment
Top Group: Go Science
Top Player: Z7ro
Top Score: 10,442
Categories: Design, Overall
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 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!
Puzzle
Expires: 04/28/17 23:00:00
Top Group: Anthropic Dreams
Top Player: Galaxie
Top Score: 9,164
Categories: Overall, Prediction
This is a domain of the human dysferlin protein. Dysferlin is found in muscle cells and associates with the cell membrane, although its exact function is unknown. Mutations in the dysferlin gene can cause a debilitating type of muscular dystrophy. See the blog for more info. Our collaborators at the Jain Foundation would like to model the structure of dysferlin to better understand its function, and have asked Foldit players to help! Players may recall folding the C2B calcium-binding domain of dysferlin in Puzzles 1291 and 1293b. The residues modeled in this puzzle link two calcium-binding domains in dysferlin. It is unclear whether this domain serves a particular function, but some experimental data suggests it is well-folded.
Puzzle
Expires: 06/01/17 23:00:00
Top Player: anthion
Top Score: 8,520
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
Expires: 06/01/17 23:00:00
Top Group: PSU Berks BMB 465
Top Player: anthion
Top Score: 8,682
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
Expires: 05/25/17 23:00:00
Top Group: D001x Med Chem MOOC
Top Player: anthion
Top Score: 10,218
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
Expires: 05/25/17 23:00:00
Top Group: Go Science
Top Player: anthion
Top Score: 10,194
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
Expires: 05/18/17 23:00:00
Top Group: Jayisgames
Top Player: anthion
Top Score: 8,918
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
Expires: 05/18/17 23:00:00
Top Group: STME 5240
Top Player: WalkerP
Top Score: 8,955
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.
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Supported by: UW Center for Game Science, UW Department of Computer Science and Engineering, UW Baker Lab, VU Meiler Lab,
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