Foldit Puzzles

1894: Symmetric Trimer Design: H-bond Networks

Design a symmetric protein trimer, with 3 identical chains that assemble together! Note the Interaction Energy Objective, which will penalize poorly-scoring large residues that can lead to unwanted protein aggregation. The H-bond Network Objective encourages players to build buried, 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! We've also adjusted the H-bond Network Objective so that poor-scoring H-bonds may not contribute to networks; poor-scoring H-bonds will be displayed in red. This puzzle uses the Buried Unsats Objective, with a large penalty for buried polar atoms that can't make H-bonds. In this puzzle, there are no limits on the Complex Core, but we've included the Complex Core objective so players can see the core residues that can be incorporated into H-bond Networks.

1893: Revisiting Puzzle 137: Rosetta Decoy

This is a throwback puzzle to the early days of Foldit. This protein helps to regulate the human immune response, and the starting structure is a Rosetta model. The protein is modeled here in the 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 and to provide newer players with puzzles that are still scientifically relevant.

1892: Coronavirus Binder Design: Round 18

Design a binder against coronavirus! The new metrics have been left out to preserve regular recipe performance, but other Objectives are still in effect. Remember, if your designed protein creates Buried Unsats, then it will be less likely to fold and bind to the coronavirus target. (Note that this target protein includes 8 buried unsats that players may be unable to fix.) See the blog for more details about buried unsats, and for helpful tips to make a successful protein binder! Players may not load solutions from previous puzzles.

Sandbox Puzzle 1892 with Binder Metrics

This is a non-competitive version of Puzzle 1892, with binder metric Objectives so that players can check the DDG, SASA, and shape complementarity of their Puzzle 1889 solutions. The binder metric Objectives do not award any bonus or penalties. Players may share solutions freely between this puzzle and the original Puzzle 1892.

1891: Symmetric Trimer Design: H-bond Networks

Design a symmetric protein trimer, with 3 identical chains that assemble together! Note the Interaction Energy Objective, which will penalize poorly-scoring large residues that can lead to unwanted protein aggregation. The H-bond Network Objective encourages players to build buried, 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! We've also adjusted the H-bond Network Objective so that poor-scoring H-bonds may not contribute to networks; poor-scoring H-bonds will be displayed in red. This puzzle uses the Buried Unsats Objective, with a large penalty for buried polar atoms that can't make H-bonds. In this puzzle, there are no limits on the Complex Core, but we've included the Complex Core objective so players can see the core residues that can be incorporated into H-bond Networks.

1890: Revisiting Puzzle 136: Cell Adhesion

This is a throwback puzzle to the early days of Foldit. This small protein, from the venom of the saw-scaled viper, interferes with the cellular adhesion machinery that allows blood clotting. 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.

1889: Coronavirus Anti-inflammatory Design: Round 12

Design an anti-inflammatory protein for COVID-19! We'd like players to keep focusing on making closely-packed interfaces with no extra Buried Unsats. This puzzle prohibits SER and THR in helices, which may make it harder to satisfy BUNS, but should help the helices to fold correctly. Remember, if your designed protein creates Buried Unsats, then it will be less likely to fold and bind to the target. (Note that this target protein includes 15 buried unsats that players may be unable to fix.) See the blog for more details about buried unsats, and for helpful tips to make a successful protein binder! Players will be unable to load solutions from previous puzzles.

Sandbox Puzzle 1889 with Binder Metrics

This is a non-competitive version of Puzzle 1889, with binder metric Objectives so that players can check the DDG, SASA, and shape complementarity of their Puzzle 1889 solutions. The binder metric Objectives do not award any bonus or penalties. Players may share solutions freely between this puzzle and the original Puzzle 1889.

1888: Symmetric Trimer Design: H-bond Networks

Design a symmetric protein trimer, with 3 identical chains that assemble together! Note the Interaction Energy Objective, which will penalize poorly-scoring large residues that can lead to unwanted protein aggregation. The H-bond Network Objective encourages players to build buried, 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! We've also adjusted the H-bond Network Objective so that poor-scoring H-bonds may not contribute to networks; poor-scoring H-bonds will be displayed in red. This puzzle uses the Buried Unsats Objective, with a large penalty for buried polar atoms that can't make H-bonds. In this puzzle, there are no limits on the Complex Core, but we've included the Complex Core objective so players can see the core residues that can be incorporated into H-bond Networks.

1887: Refinement Target: R1091

CASP14 has released this refinement target without any accuracy estimates, so we're unsure how well the starting structure matches the native structure. Look for better scoring folds to find the true native structure!