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Puzzle
Expired: 12/28/17 23:00:00
Top Group: Hun-Magyar Csapat
Top Player: Master of Games
Top Score: 8,715
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: 11/29/17 23:00:00
1 comment
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 22,831
Categories: Design, Overall
This is the third puzzle of our Aflatoxin Challenge, with the aflatoxin ligand now in a different orientation in the enzyme binding pocket. 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. To encourage interactions with the ligand, all ligand scores are doubled. Previous Aflatoxin Challenge designs are incompatible with this puzzle, so players will not be able to load work from previous puzzles.
Puzzle
Expired: 11/20/17 23:00:00
1 comment
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 10,768
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: 12/21/17 23:00:00
Top Group: Gargleblasters
Top Player: sansyo
Top Score: 10,979
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: 11/15/17 23:00:00
1 comment
Top Group: Go Science
Top Player: Azukay
Top Score: 10,114
Categories: Experimental
The misfolding and aggregation of amyloid proteins underlies many diseases, including Alzheimer’s disease, Parkinson’s disease, and ALS. However, the process by which protein misfolding causes cell toxicity and death is still heavily debated. In this puzzle, players are provided with three copies of the Aβ peptide, which forms amyloid fibrils in the brains of those afflicted with Alzheimer’s disease. In addition to amyloid fibrils, Aβ is known to form small soluble clusters. There is some evidence that these small clusters are more toxic than the amyloid fibrils, but the structure of such Aβ clusters is still unknown. In this puzzle, players can explore the different possibilities for how these small clusters of Aβ might fold.
Puzzle
Expired: 11/13/17 23:00:00
Top Group: Anthropic Dreams
Top Player: Galaxie
Top Score: 10,116
Categories: Overall, Prediction
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!
Puzzle
Expired: 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.
Puzzle
Expired: 11/08/17 23:00:00
13 comments
Top Group: Go Science
Top Player: Bruno Kestemont
Top Score: 13,658
Categories: Overall
This is a follow-on puzzle of Puzzle 1441: Y1 Receptor Homology Modeling. In the previous puzzle, we asked you to model the structure of the human Y1 neuropeptide receptor. In this puzzle, we'd like you to determine how a known binder of Y1 interacts with that model.

Puzzle
Expired: 11/14/17 23:00:00
10 comments
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 16,074
Categories: Design, Overall
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 1440.
Puzzle
Expired: 11/06/17 23:00:00
1 comment
Top Group: Go Science
Top Player: ZeroLeak7
Top Score: 10,147
Categories: Overall, Prediction
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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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