Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
-
This is a followup to Puzzle 1344. The score function for this puzzle has been adjusted to allow buried polar residues and exposed hydrophobics. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets! Players will be able to load in manual saves from Puzzle 1344 and use them as a starting point here.
-
This puzzle is similar to recent design puzzles except that we've restricted the use of SER and THR residues in α-helices. Foldit players have submitted some stellar-looking designs recently, but we are seeing quite a lot of SER and THR residues in designed helices. Recent experiments in our lab suggest that these residues are somewhat unfavorable in helices, so in this puzzle we've restricted the use of SER and THR in helical positions. See the puzzle comments for filter 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!
-
This is a throwback puzzle to the early days of Foldit. This small domain is part of a larger protein found at high concentrations of the lens of the eye; historically, this protein was purified from the eyes of B. taurus for research. The protein is modeled here in 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.
-
The structure of this protein is still unknown. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!
-
This is a repost of Puzzle 1340, now with an electron density map! This protein is secreted at the site of inflammation, recruiting monocytes and T cells to help fight an infection. This protein contains four cysteine residues that oxidize to form two disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been. Players may load in solutions from Puzzle 1340.
-
The Ideal Loop Filter is back, but we've made some changes to encourage more proline residues. The Blueprint panel is still available, which can be accessed from the Actions menu (or the Main menu in Selection Interface). Like other recent puzzles, the Rebuild action has been disabled here; in its place we encourage players to use Remix instead. See the puzzle comments for filter 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!
-
The structure of this protein is still unknown. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!
-
This is a throwback puzzle to the early days of Foldit. This protein is secreted at the site of inflammation, recruiting monocytes and T cells to help fight an infection. This protein contains four cysteine residues that oxidize to form two disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
-
The Ideal Loop Filter is back, but we've made some changes to encourage more proline residues. The Blueprint panel is still available, which can be accessed from the Actions menu (or the Main menu in Selection Interface). Like other recent puzzles, the Rebuild action has been disabled here; in its place we encourage players to use Remix instead. See the puzzle comments for filter 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!
-
The structure of this protein is still unknown. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!