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Puzzle
Expires: 12/19/17 18:00:00
Top Group: Anthropic Dreams
Top Player: hansvandenhof
Top Score: 9,941
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
Expires: 12/18/17 23:00:00
1 comment
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 10,081
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!
Puzzle
Expires: 01/18/18 23:00:00
Top Group: L'Alliance Francophone
Top Player: pizpot
Top Score: 14,203
Categories: Beginner
In electron density puzzles, we give you some experimental data to help you find the correct fold. This data takes the form of an electron density, and appears in game as a guide. You can adjust the guide visualization by going to [Actions]>[Electron Density]. For players with fewer than 150 global points.
Puzzle
Expires: 01/11/18 23:00:00
Top Group: Richard Dawkins Foundation
Top Player: flemdogmillionaire
Top Score: 8,413
Categories: Beginner
We are giving you this Parabacteroides Distasonis protein as an extended chain. The native is shown as a guide on this puzzle, so try using everything you have learned in the Intro levels to match the native fold. Hints and details are posted in the puzzle comments. For players with fewer than 150 global points.
Puzzle
Expires: 12/13/17 23:00:00
3 comments
Top Group: Anthropic Dreams
Top Player: tokens
Top Score: 23,106
Categories: Design, Overall
This is the fourth puzzle of our Aflatoxin Challenge; now players may insert and delete residues in solutions from the previous Round 3 puzzle. Aflatoxins are a class of poisonous compounds that contaminate a significant portion of the global food supply. In this puzzle, players are challenged to redesign an enzyme that could break down aflatoxin molecules. The majority of the protein is frozen, with the aflatoxin ligand fixed in a binding pocket. Surrounding the binding pocket are a number of loops that might be redesigned without affecting the folding stability of the protein. In these loops, players may manipulate the protein backbone and mutate the residue sidechains. Players may add up to 20 additional residues within these loops, at a cost of 16 points per residue. Players may load in solutions from Puzzle 1450.
Puzzle
Expires: 01/04/18 23:00:00
Top Group: Hun-Magyar Csapat
Top Player: Osiris
Top Score: 8,633
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: 12/28/17 23:00:00
Top Group: Hun-Magyar Csapat
Top Player: Master of Games
Top Score: 8,689
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: 12/21/17 23:00:00
Top Group: Hun-Magyar Csapat
Top Player: flemdogmillionaire
Top Score: 10,939
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: 12/14/17 23:00:00
Top Group: Hun-Magyar Csapat
Top Player: histon
Top Score: 8,963
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.

Closed

Puzzle
Expired: 12/11/17 23:00:00
1 comment
Top Group: Gargleblasters
Top Player: Enzyme
Top Score: 11,118
Categories: Design, Overall
This puzzle challenges players to design a protein with 95-120 residues. We've softened the penalties associated with the Core Existence and Residue Count filters, which have typically been very steep. The starting structure has 95 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, Microsoft, Adobe, RosettaCommons