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This puzzle challenges players to design a single-chain protein with 75-90 residues. We've softened the penalties associated with the Core Existence filter, which have typically been very steep. The starting structure has 75 residues, but more can be added at a cost of 23 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!

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 small unsolved Arabidopsis protein only has 59 residues and negatively controls the biosynthesis of starch in plants and regulates leaf and seed composition. We are giving you 5 starts for this puzzle. Resetting the puzzle will cycle through these 5 Zhang server predictions. They are also in the Alignment Tool so you can use partial threading as well as an extended chain. For players with fewer than 150 global points.

This is a throwback puzzle to the early days of Foldit. This pilin protein allows the P. aeruginosa bacterium to adhere to human cells, sometimes resulting in infection. The starting structure is a Rosetta model. This protein contains two cysteine residues which oxidize to form one disulfide bond. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

This puzzle challenges players to design a single-chain protein with 85-105 residues. In this design puzzle, we've deactivated the Ideal Loops filter, so players have more flexibility to design their own high-scoring loops! The starting structure has 85 residues, but more can be added at a cost of 23 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!

Note: This puzzle will crash Foldit on Linux operating systems, due to a known bug related to electron density. For this reason, the puzzle is worth 0 points, and players should not feel compelled to play this puzzle to remain competitive on the leaderboards. Nevertheless, we are quite invested in this protein, and would appreciate any help from Foldit players to build a better model into this electron density map!

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 is a throwback puzzle to the early days of Foldit. This human protein helps to regulate the reduction potential of the cell, and should be modeled here in reduced form (without disulfides bonds). We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

Like Puzzle 1473, this puzzle lacks the regular design filters, although many of the design tools have been restored (i.e. Remix, Rama Map, Blueprint Panel). Foldit has changed a great deal since we ran the first Foldit design puzzle, back in August of 2009, and the results of recent design puzzles have shown that Foldit players are now perfectly capable of designing well-folded, stable proteins. We'd like to write up a paper about these results, and it will be important to have a clear picture of what happens without those special tools and filters now used for protein design. We're asking Foldit players to forget everything you've learned about protein design! This puzzle uses only a basic Rosetta scoring function, and we do not expect top-scoring designs to be realistic. But we're very curious whether Foldit players will find the same solutions as back in 2009. What is the best-scoring structure you can come up with without the design filters?

This is another protein designed by Foldit players! We've been able to purify and crystallize this protein, which was designed by tokens in Puzzle 1313. The protein crystal diffracts x-rays to a resolution of 1.9 Å, and we've been able to derive an electron density map for the crystal. We think we have a pretty good idea of this protein's structure from the electron density, but some data analysis suggests our model could be improved. We want to know if Foldit players can build a better model into the electron density!