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This is the ninth puzzle in the poly-proline helix design series! The starting structure is still a 90 residue protein with a 6 residue helix. All residues are mutable, and keeping all buried polars satisfied remains a key component of a good structure, as is a hydrophobic core and well defined secondary structures. We should be introducing a score filter very soon which will allow you to see what atoms are problematic. This should be a big help to Foldit players!

This symmetric design puzzle has C3 symmetry, with three symmetric chains. This a Sketchbook puzzle with a Move Limit of 250 moves! After that, you will be unable to improve your solution, but you can restart the puzzle to reset your move count! The Move Limit is meant to encourage players to try lots of different folds, and we hope this will increase the diversity of player solutions. This puzzle is also a little different from other symmetry puzzles, in that we want players to focus on building a smaller interface between the chains. The "Core Limit: Complex" objective will incur penalties if there are too many buried residues in the total assembly. See the puzzle comments for Objective 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. In the struggle for limited resources, some strains of the bacteria E. coli produce a potent toxin to fight off competing strains. This small immunity protein protects the aggressor E. coli from falling victim to its own toxin. 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 easier puzzles that are still scientifically relevant.

Fold the transposase protein into a density map! This is a followup to Puzzle 1787: CRISPR-Cas Transposase Part II, now with a cryo-EM density map! Players may load in previous work from Puzzle 1787.

This symmetric design puzzle has C3 symmetry, with three symmetric chains. This puzzle reintroduces the Move Limit! After 250 moves, you will be unable to improve your solution, but you can restart the puzzle to try a new fold! The Move Limit is meant to encourage players to try lots of different folds, and we hope this will increase the diversity of player solutions. This puzzle is also a little different from other symmetry puzzles, in that we want players to focus on building a smaller interface between the chains. The "Core Limit: Complex" objective will incur penalties if there are too many buried residues in the total assembly. See the puzzle comments for Objective 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 is found on the surface of bacteriophage fd, a virus that infects E. coli. It is responsible for penetrating the cell membrane of the host bacteria, allowing virus to enter the cell. This protein contains four cysteines 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, and to provide newer players with easier puzzles that are still scientifically relevant.

Fold the transposase protein into a density map! This is a followup to Puzzle 1784: CRISPR-Cas Transposase Part I, now with a cryo-EM density map! Players may load in previous work from Puzzle 1784.

Design a symmetric trimer, with 3 identical chains that assemble together! This puzzle includes a Secondary Structure Objective so that no more than 50% of residues may form helices. The H-bond Network Objective encourages players to bury satisfied H-bond networks at the interface between symmetric chains. H-bond networks are a great way to introduce polar residues at the interface, but it's important that all of the bondable atoms make hydrogen bonds! In this puzzle, there are no limits on the Complex Core, but we've included the Complex Core objective so players can see which residues count as core in the H-bond Networks.

This is a throwback puzzle to the early days of Foldit. This small disulfide-rich protein is produced by the moth H. virescens as a defense against certain bacterial and fungal infections. This protein contains six cysteines that oxidize to form three disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

This is the eighth puzzle in the poly-proline helix design series! The starting structure is slightly longer than previous rounds, with a 90 residue protein and a 6 residue helix. All residues are mutable, and we have reset the proline reference energy to 16.4 to allow for a greater diversity of residues. Keeping all buried polars satisfied is still a key component of a good structure, as well as a hydrophobic core and well defined secondary structures.