Closed

This is a throwback puzzle to the early days of Foldit. This small peptide was discovered in platypus venom-a rare instance of mammalian-produced venom, although this peptide appears similar to more widespread antimicrobials. This protein contains six cysteine residues 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 symmetric design puzzle has C3 symmetry, with three symmetric chains. This puzzle is 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!

Design a protein that binds IL-7R!

This is a throwback puzzle to the early days of Foldit. This domain is a component of a large glycoprotein in humans that has been linked to autosomal dominant polycystic kidney disease. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

Design a protein that binds IL-7R!

Design a protein that binds IL-7R!

This is a throwback puzzle to the early days of Foldit. This short protein is a component of the α-ketoglutarate dehydrogenase complex, which is best known for its role in the citric acid cycle. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

The Aflatoxin Challenge is back! The Siegel Lab has found a new enzyme scaffold that is better suited to degrade the aflatoxin molecule, and they're asking Foldit players to redesign the enzyme so that it can bind aflatoxin more strongly! Players may insert up to 10 extra residues into two designable loops, at a cost of 20 points per residue. Players may also mutate the sidechains at positions 122 and 123, where the backbone is fixed. Parts of the scaffold protein have been trimmed to reduce the size of the puzzle, and we've upweighted ligand interactions by a factor of five. We'd like to see if Foldit players can design proteins that make more interactions with the ligand! See the blog for more details.

Note: This puzzle replaces Puzzle 1738, which had errors with the frozen binding helices. Unfortunately, players will not be able to load solutions from Puzzle 1738.

Note: This puzzle was closed early due to an error with the frozen binding helices. The puzzle has been reposted as Puzzle 1738b. Players will not be able to load solutions into the reposted puzzle.