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Puzzle
Expires: 09/26/14 23:00:00
Top Group: Another Hour Another Point
Top Player: Aotearoa
Top Score: 8,409
Categories: Overall, Prediction
Our preliminary analysis suggests that very few players were able to improve the starting model of this CASP11 refinement target from Puzzle 924. We'd like to see if you can reach the native structure for this CASP refinement target when it's provided as a guide. Players may NOT load in solutions from Puzzle 924.
Puzzle
Expires: 10/30/14 23:00:00
Top Group: WPI CH4110
Top Player: azak2002
Top Score: 14,483
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: 09/23/14 23:59:00
1 comment
Top Group: Anthropic Dreams
Top Player: jamiexq
Top Score: 13,367
Categories: Overall, Predicted Contacts, Prediction
This contact map puzzle is based on the same CASP11 target as Puzzle 962, but the threshold distance for contacts has been relaxed. Contacts are scored with the Contact Map filter in this puzzle, and there is an upper limit of 4300 possible points from the filter. Players will NOT be able to load solutions from Puzzle 962.
Puzzle
Expires: 09/22/14 23:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: Galaxie
Top Score: 9,548
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This toxic peptide is a potent anti-coagulant that inhibits cell adhesion, and is found in the venom of saw-scaled vipers. Players will receive a bonus for forming up to four disulfide bonds in this puzzle. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been. Players will NOT be able to load in any previous solutions for these puzzles.
Puzzle
Expires: 10/23/14 23:00:00
Top Group: Anthropic Dreams
Top Player: jen.sweny
Top Score: 8,643
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: 10/16/14 23:00:00
Top Group: SETI.Germany
Top Player: teraflop
Top Score: 8,682
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: 10/09/14 23:00:00
2 comments
Top Group: Anthropic Dreams
Top Player: superbro
Top Score: 8,800
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: 10/02/14 23:00:00
Top Group: WPI CH4110
Top Player: FHRITP
Top Score: 11,150
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: 09/25/14 23:00:00
Top Group: SETI.Germany
Top Player: teraflop
Top Score: 9,276
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: 09/19/14 23:00:00
6 comments
Top Group: Beta Folders
Top Player: smilingone
Top Score: 16,170
Categories: Design, Overall
We've been posting puzzles to try to design an Abeta-binding protein. Abeta is the polypeptide that's responsible for Alzheimer's disease, and we hope that something that's able to bind up Abeta could be useful for preventing it from aggregating and causing neurotoxic effects. The first full-length Abeta design puzzle (puzzle 976) produced some very interesting designs -- particularly among the solutions that were shared with scientists. We've selected one of these for refinement in this puzzle. Congratulations to saksoft2, gitwut, and the Contenders for this design.

While the topology is interesting, it's not quite where we want it to be, yet. In this puzzle, we'd like everyone to try to improve this design. Pay particular attention to:

--Voids. Though the scoring function doesn't always penalize voids as much as it should, we can't stress enough how important it is to have well-packed protein cores and interfaces that are free of holes. (It's a good idea to turn on the void display in the advanced view options.) We have activated the core existence filter, so you'll get more points for having a nice, well-packed hydrophobic core.

--Disulfide bonds. Disulfides connecting parts of the protein that are far apart in linear sequence are particularly stabilizing. There are three disulfides in the starting conformation, but they're not in great places. You'll get bonus points for forming up to four disulfide bonds. Try to tie separate elements of secondary structure together with these linkages.

--Regions with not-so-great geometry. In this structure, the ends of the protein in particular aren't doing much. You can rebuild these, or cut them off and place new residues elsewhere in the structure.

--Hydrophobic residue burial. There are some hydrophobic (particularly on the Abeta peptide) that are sticking out into water. We'd like to bury those if we can.
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