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Puzzle
Expired: 04/14/22 18:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: LociOiling
Top Score: 9,863
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This protein comes from the bacteria Escherichia coli, but its function is still unknown! 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.
Puzzle
Expired: 04/13/22 23:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: Galaxie
Top Score: 19,287
Categories: Design, Overall, Symmetry
Design a symmetric protein trimer, with 3 identical chains of 60 residues each! This puzzle enables AlphaFold predictions for the monomer subunit of your design, so you can upload your solution for AlphaFold using the AlphaFold prediction tool. AlphaFold will predict the structure of your monomer subunit only (i.e. in the unbound state, in the absence of other symmetric copies). If you load this prediction, then Foldit will attempt to align the prediction with your solution. If you continue working off of the AlphaFold prediction, you may need to make adjustments at the interface where the monomer subunit interacts with symmetric copies.
Puzzle
Expired: 04/30/22 23:00:00
8 comments
Top Group: Anthropic Dreams
Top Player: LociOiling
Top Score: 12,658
Categories:
This sandbox puzzle features three successful protein binders designed by scientists in this recent research paper. There are three starting structures, showing designed binders for CD3-delta, FGF receptor 2, and IGF1 receptor. Reset the puzzle to cycle through the different starting structures.
Puzzle
Expired: 04/08/22 23:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: Galaxie
Top Score: 11,285
Categories: Design, Overall
Design a protein to bind to the Tie2 receptor! This puzzle has a reduced BUNS penalty so that players can focus on other Objectives--but don't forget about BUNS completely! This puzzle enables AlphaFold predictions for your designed binder. Once you've designed a binder for the target, upload your solution for AlphaFold using the AlphaFold prediction tool. AlphaFold will predict the structure of your binder chain only (i.e. in the unbound state, in the absence of the target). If you load this prediction, then Foldit will attempt to align the prediction with your solution (i.e. in the bound state, making an interface with the target). If you continue working off of the AlphaFold prediction, you may need to make adjustments at the interface where the binder interacts with the target.
Puzzle
Expired: 04/30/22 23:00:00
Top Group: Go Science
Top Player: toshiue
Top Score: 23,722
Categories:
This sandbox puzzle features a symmetric tetramer design by BootsMcGraw in Puzzle 2121. This design uses an extensive H-bond Network to satisfy buried polar residues at the symmetric interface.
Puzzle
Expired: 04/30/22 23:00:00
1 comment
Top Group: Go Science
Top Player: toshiue
Top Score: 12,478
Categories:
This sandbox puzzle features three successful protein binders designed by scientists in this recent research paper. There are three starting structures, showing designed binders for CD3-delta, FGF receptor 2, and IGF1 receptor. Reset the puzzle to cycle through the different starting structures.
Puzzle
Expired: 04/07/22 18:00:00
1 comment
Top Group: Go Science
Top Player: Bruno Kestemont
Top Score: 10,694
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This protein shuttles lipids between cell membranes in the rice plant. The protein contains eight cysteines 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 and to provide newer players with problems that are still scientifically relevant.
Puzzle
Expired: 04/06/22 23:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: Galaxie
Top Score: 22,047
Categories: Design, Overall, Symmetry
Design a symmetric protein trimer, with 3 identical chains of 80 residues each! This puzzle enables AlphaFold predictions for the monomer subunit of your design, so you can upload your solution for AlphaFold using the AlphaFold prediction tool. AlphaFold will predict the structure of your monomer subunit only (i.e. in the unbound state, in the absence of other symmetric copies). If you load this prediction, then Foldit will attempt to align the prediction with your solution. If you continue working off of the AlphaFold prediction, you may need to make adjustments at the interface where the monomer subunit interacts with symmetric copies.
Puzzle
Expired: 04/01/22 23:00:00
1 comment
Top Group: Contenders
Top Player: dcrwheeler
Top Score: 14,284
Categories: Design, Overall
Design a protein that can bind to CD22! This puzzle has a reduced BUNS penalty so that players can focus on other Objectives--but don't forget about BUNS completely! This puzzle enables AlphaFold predictions for your designed binder. Once you've designed a binder for the target, upload your solution for AlphaFold using the AlphaFold prediction tool. AlphaFold will predict the structure of your binder chain only (i.e. in the unbound state, in the absence of the target). If you load this prediction, then Foldit will attempt to align the prediction with your solution (i.e. in the bound state, making an interface with the target). If you continue working off of the AlphaFold prediction, you may need to make adjustments at the interface where the binder interacts with the target.
Puzzle
Expired: 03/31/22 18:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: LociOiling
Top Score: 10,876
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This protein allows bacteria to metabolize ethanolamine and use it in constructing cell walls and cell membranes. The protein is modeled here in reduced form, 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.
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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, Boehringer Ingelheim, RosettaCommons