Puzzles Feed

Closed

Puzzle
Expired: 07/16/18 19:00:00
1 comment
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 11,659
Categories: Pilot
This protein has 92 residues! It was designed by the Baker Lab in 2003, and has a topology unlike any natural protein yet discovered. In this experimental puzzle you will have 256 moves at your disposal. Once you use them up, you can reset and try something else!
Puzzle
Expired: 07/12/18 23:00:00
1 comment
Top Group: Contenders
Top Player: georg137
Top Score: 9,993
Categories: Pilot
These are the two chains of a bio-engineered variant of human insulin, which contains six cysteine residues that oxidize to form three disulfide bonds. In this experimental puzzle you will have 128 moves at your disposal. Once you use them up, you can reset and try something else!
Puzzle
Expired: 07/10/18 23:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: Waya
Top Score: 11,414
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 32 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: 07/09/18 20:00:00
Top Group: Void Crushers
Top Player: fiendish_ghoul
Top Score: 10,480
Categories: Pilot
Note: This puzzle replaces Puzzle 1542 which was closed early due to a bug.
Puzzle
Expired: 07/08/18 23:00:00
2 comments
Top Group: Void Crushers
Top Player: Timo van der Laan
Top Score: 9,203
Categories:
Note: This puzzle was closed early due to a missing filter file resulting in no bonuses being received for forming disulfide bonds. It is superseded by Puzzle 1542b. Players may load their work from this puzzle into the reposted puzzle.
Puzzle
Expired: 07/09/18 18:00:00
1 comment
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 9,217
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This short protein is a component of the α-ketoglutarate dehydrogenase complex, which is best known for its role in the citric acid cycle. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
Puzzle
Expired: 07/03/18 23:00:00
1 comment
Top Group: Beta Folders
Top Player: smilingone
Top Score: 11,993
Categories: Design, Overall
This puzzle challenges players to design a single-chain protein with 85-105 residues. The starting structure has 85 residues, but more can be added at a cost of 32 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: 07/02/18 18:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: Galaxie
Top Score: 11,216
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This protein is found in high concentrations in the lens of the eye. Among its other functions, it is responsible for the high refractive index (and resulting optical properties) of the lens. The protein is modeled here in 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.
Puzzle
Expired: 07/06/18 23:00:00
2 comments
Top Group: Contenders
Top Player: Bletchley Park
Top Score: 14,045
Categories: Design, Overall
Redesign the active site to bind aflatoxin! This puzzle is much like Round 7 of the Aflatoxin Challenge, but now the aflatoxin molecule is no longer frozen, and can be moved within the active site. Strong constraints will keep aflatoxin from moving too far from its starting position, but we think the extra wiggle room will allow Foldit players to design an active site that binds the molecule more tightly. Although no extra residues may be inserted in this puzzle, players may remove residues at positions 62-67, which clash with the aflatoxin molecule. Parts of the scaffold protein have been trimmed to reduce the size of the puzzle, and we've upweighted ligand interactions by a factor of five. We'd like to see if Foldit players can design proteins that make more interactions with the ligand! See the blog for more details.
Puzzle
Expired: 06/28/18 23:00:00
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 10,793
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, Amazon, Microsoft, Adobe, RosettaCommons