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Puzzle
Expired: 01/08/20 18:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: grogar7
Top Score: 11,104
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This protein, isolated from the hookworm A. caninum, is an extremely potent anticoagulant. This protein contains ten cysteine residues that oxidize to form five disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
Puzzle
Expired: 01/03/20 23:00:00
2 comments
Top Group: Anthropic Dreams
Top Player: grogar7
Top Score: 23,612
Categories: Design, Overall, Symmetry
Design a symmetric tetramer, with 4 identical chains that assemble together! The H-bond Network Objective encourages players to bury satisfied H-bond networks at the interface between symmetric chains. H-bond networks are a great way to introduce polar residues at the interface, but it's important that all of the bondable atoms make hydrogen bonds! In this puzzle, there are no limits on the Complex Core, but we've included the Complex Core objective so players can see which residues count as core in the H-bond Networks.
Puzzle
Expired: 01/02/20 23:00:00
8 comments
Top Group: Contenders
Top Player: Bletchley Park
Top Score: 11,330
Categories: Design, Overall
This is the fifth puzzle in the poly-proline helix design series! We have shortened the helix to six residues while keeping the 80 residue protein that you are familiar with to make it easier to satisfy the polar atoms. All residues are mutable. We want satisfying the buried oxygens on the helix with hydrogen bonds to be a priority because if they are not, then the protein cannot fold. We hope to introduce a buried polars score filter soon to help you identify which residues are buried. Until then, hydrogen bonds are visible by selecting 'Show advanced GUI' in General Options in the Menu tab, and then selecting 'Show bonds (loop)' and 'Show bondable atoms' in the View tab.
Puzzle
Expired: 01/01/20 18:00:00
1 comment
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 9,915
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This small domain is part of a larger protein that mediates interactions between other proteins in human development. This protein contains several cysteine residues, but we are modeling them in a reducing environment, so they should NOT form disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
Puzzle
Expired: 12/27/19 23:00:00
4 comments
Top Group: Beta Folders
Top Player: retiredmichael
Top Score: 20,592
Categories: Design, Overall, Symmetry
Design a symmetric tetramer, with 4 identical chains that assemble together. The H-bond Network Objective encourages players to bury satisfied H-bond networks at the interface between symmetric chains. H-bond networks are a great way to introduce polar residues at the interface, but it's important that all of the bondable atoms make hydrogen bonds! In this puzzle, there are no limits on the Complex Core, but we've included the Complex Core objective so players can see which residues count as core in the H-bond Networks.
Puzzle
Expired: 12/26/19 23:00:00
1 comment
Top Group: Gargleblasters
Top Player: Enzyme
Top Score: 11,134
Categories: Design, Overall
This is the fourth puzzle in the poly-proline helix design series! The starting structure is identical to the one in round 3, with an 80 residue protein and an 8 residue helix. The backbone will be frozen to maintain the poly-proline helix secondary structure, but we are now giving you free rein to design the residues on the helix. We want to see how you will satisfy the exposed oxygens on the helix backbone, because proteins that satisfy all internal oxygens with hydrogen bonds have the best chance of folding in the lab.
Puzzle
Expired: 12/25/19 18:00:00
1 comment
Top Group: Go Science
Top Player: silent gene
Top Score: 9,833
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This toxin, which is released by the sea anemone A. xanthogrammica, disrupts normal contraction of cardiac muscle in potential predators, and furthermore serves as a pheromone to signal danger to nearby anemones. This protein contains six cysteine residues 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
Expired: 12/20/19 23:00:00
3 comments
Top Group: Gargleblasters
Top Player: Enzyme
Top Score: 22,885
Categories: Design, Overall, Symmetry
H-bond Networks are back! The H-bond Network Objective encourages players to bury satisfied H-bond networks at the interface between symmetric chains. H-bond networks are a great way to introduce polar residues at the interface, but it's important that all of the bondable atoms make hydrogen bonds! In this puzzle, there are no limits on the Complex Core, but we've included the Complex Core objective so players can see which residues count as core in the H-bond Networks.
Puzzle
Expired: 12/19/19 23:00:00
7 comments
Top Group: Go Science
Top Player: silent gene
Top Score: 11,695
Categories: Design, Overall
This is the third puzzle in our poly-proline helix design series! This is an 80 residue protein with a shorter 8-residue long frozen poly-proline helix, and designable residues on either side. Just like in Rounds 1 and 2, it will be necessary to satisfy the exposed oxygens on the helix backbone to ensure that the protein stays folded! Globular structures with a hydrophobic core will have the best chance of folding in the real world.
Puzzle
Expired: 12/18/19 18:00:00
1 comment
Top Group: Go Science
Top Player: silent gene
Top Score: 10,408
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This toxin, produced by the Chinese cobra N. atra, induces contracture in skeletal and cardiac muscle. This protein contains eight cysteine residues that oxidize to form four disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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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