Closed

Note: This puzzle replaces the original Puzzle 1515, which was posted with an erroneous Residue Count Filter. Players may load their saved work from the original Puzzle 1515.

This is a small symmetric trimer design puzzle. A symmetric protein relies not only on how well folded each part is, but also on how well they interface together. Your changes will be reflected in the symmetric unit. Make sure you have completed Intro Puzzle 5-2, and 7-1 through 7-4. For players with fewer than 150 global points.

This puzzle features a protein designed by fiendish_ghoul in Puzzle 1331! Last week, we challenged players to try to predict the structure of this protein from the sequence alone, in Puzzle 1511. We have since solved the crystal structure of this protein, and here we are providing players with the refined electron density map at a resolution of 1.54 Å. The crystal's electron density shows that this protein folds up exactly as fiendish_ghoul designed it, with RMSD of 0.9 Å among Cα atoms! Players can load in solutions from Puzzle 1511 to see how their predictions fit in the electron density map, or players can try building into the electron density from an extended chain.

Note: This puzzle was closed early due to an erroneous Residue Count Filter, and reposted as Puzzle 1515b. Players may load their work from this puzzle into the reposted puzzle.

This is a throwback puzzle to the early days of Foldit. This protein is able to absorb light and use the energy to transfer chloride ions across the cell membrane. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

This is a small symmetric trimer design puzzle. A symmetric protein relies not only on how well folded each part is, but also on how well they interface together. Your changes will be reflected in the symmetric unit. Make sure you have completed Intro Puzzle 5-2, and 7-1 through 7-4. For players with fewer than 150 global points.

This puzzle challenges players to design a single-chain protein with 95-120 residues. The starting structure has 95 residues, but more can be added at a cost of 32 points per residue. 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 protein was designed by the Baker Lab in 2003, and has a topology unlike any natural protein yet discovered. 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!

We are giving you a helix positioned over a hydrophobic groove where binding occurs in nature. You can mutate any residue on the helix but none on the native binding region. Try to look for favorable hydrophobic interactions in this groove while maintaining the helix. For players with fewer than 150 global points.