Closed

Note: Due to an error with the BUNS Objective, this puzzle was closed early and reposted as Puzzle 1912b.

This sandbox puzzle features a symmetric trimer design by CharlieFortsConscience, from Puzzle 1900. It is difficult to form a well-shaped trimer interface with sheets, but this design has very few voids at the interface!. For more, check out Foldit Lab Report #14 on YouTube! This sandbox puzzle is non-competitive and will not award any points.

This is a throwback puzzle to the early days of Foldit. This protein helps to regulate oxidation in the cell; the starting structure is a model produced by Rosetta. This protein contains four cysteine residues, but in this state only two of them are expected to oxidize to form a single disulfide bond. 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.

Design a binder for the viral spike of MERS-CoV! This puzzle is similar to Puzzle 1907, but now includes special Foldit Metrics for the DDG, SASA, and SC of your solution. These Metrics are slow to compute and run in the background, so gameplay may be different from regular puzzles. Each Metric has a target, players will receive a 1000 pt bonus for meeting each target. See the blog for more info about Foldit Metrics.

Design a symmetric protein tetramer, with 4 identical chains that assemble together! 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.

Refold the loops in this Aflatoxin Challenge design! In the most recent lab tests the Siegel Lab identified three well-behaved designs that show activity against aflatoxin. We want to know how these designs fold in the absence of aflatoxin. This puzzle features a protein designed by LociOiling in Puzzle 1739, but the starting structure has been partially unfolded. Help us predict the structure of this design by folding the redesigned loops!

Design a binder for the viral spike of MERS-CoV! MERS is a respiratory disease similar to COVID-19, and is caused by a related coronavirus. There have been several MERS outbreaks since 2012, but there is still no treatment has been developed for the disease. The MERS-CoV virus is coated with a spike protein that recognizes the human protein DPP4, which is found on the surface of lung cells. A protein that binds to the MERS-CoV spike could be used as a drug to block DPP4 recognition and slow viral infection.

This non-competitive sandbox puzzle features a new kind of Objective that we're calling Metrics. Metrics are slow to compute, so they are calculated in the background while you're folding your protein. That means that sometimes your score will be greyed out while the metrics are computing, but if you wait just a second then they will finish and your score will regain color. See the blog for more info about Metrics in Foldit. This is a multi-start puzzle with binders for the Coronavirus spike. You can start the puzzle with (1) a fragment of the natural ACE2 receptor, (2) the designed binder LCB1, or (3) an extended chain so you can design your own. Cycle through the different starting structures by resetting the puzzle. The puzzle Objectives include three Metrics (DDG, SASA, SC), so that you can practice designing protein binders using these binder metrics. This puzzle is non-competitive and will award no points.

Design a symmetric protein trimer, with 3 identical chains that assemble together! This puzzle includes a Secondary Structure Objective, so no more than 50% of your design can form helices. 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.

Refold the loops in this Aflatoxin Challenge design! In the most recent lab tests the Siegel Lab identified three well-behaved designs that show activity against aflatoxin. We want to know how these designs fold in the absence of aflatoxin. This puzzle features a protein designed by Phyx in Puzzle 1739, but the starting structure has been partially unfolded. Help us predict the structure of this design by folding the redesigned loops!