Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
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For our one thousandth puzzle, we've got a particularly challenging task for you. We have posted a few past puzzles in which we have asked players to design peptides and small proteins that are able to bind to a binding site on the Ebola binding protein. The glycoprotein uses this site to latch onto a human cell membrane protein as a first step in invading host cells, which means that something binding at this site should hinder viral entry into cells.
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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. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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In natural proteins, different amino acids show different propensities for forming secondary structures like alpha helices and beta strands. This puzzle includes a new SS Design filter that restricts the use of GLY residues in helices and sheets. There are several other filters in effect; see the puzzle comments for details. The Baker Lab will run folding predictions on your solutions for this puzzle, and those that perform well will be synthesized in the lab. Remember, you can use the Upload for Scientists button for up to 5 designs that you want us to look at, even if they are not the best-scoring solutions!
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In this de-novo freestyle puzzle, the "High Wiggle Power" option has been disabled. The results from these puzzles will help us determine how useful the wiggle power options may be for structure prediction in Foldit. The secondary structure predictions are provided on the starting model, with more details posted in the puzzle comments.
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In this de-novo freestyle puzzle, the "High Wiggle Power" option has been disabled. The secondary structure predictions are provided on the starting model, with more details posted in the puzzle comments.
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In natural proteins, different amino acids show different propensities for forming secondary structures like alpha helices and beta strands. This puzzle includes a new SS Design filter that restricts the use of GLY residues in helices and sheets. There are several other filters in effect; see the puzzle comments for details. The Baker Lab will run folding predictions on your solutions for this puzzle, and those that perform well will be synthesized in the lab. Remember, you can use the Upload for Scientists button for up to 5 designs that you want us to look at, even if they are not the best-scoring solutions!
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This is a throwback puzzle to the early days of Foldit. This protein resolves aminoacyl-tRNA mismatches to reduce errors in protein translation; the starting structure is a model produced by Rosetta. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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Our preliminary analysis suggests that very few players were able to improve the starting model of this CASP11 refinement target from Puzzle 921. 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 921.
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In this de-novo freestyle puzzle, the "High Wiggle Power" option has been disabled. The secondary structure predictions are provided on the starting model, with more details posted in the puzzle comments.
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In natural proteins, different amino acids show different propensities for forming secondary structures like alpha helices and beta strands. This puzzle includes a new Secondary Structure Design filter that restricts the use of GLY residues in helices and sheets. There are several other filters in effect; see the puzzle comments for details. The Baker Lab will run folding predictions on your solutions for this puzzle, and those that perform well will be synthesized in the lab. Remember, you can use the Upload for Scientists button for up to 5 designs that you want us to look at, even if they are not the best-scoring solutions!