Foldit Puzzles

1357: Electron Density Practice: Trypsin Inhibitor

This puzzle is meant for Foldit players to practice folding a protein with an electron density map. This electron density map was generated from x-ray diffraction at a resolution of 1.5 Å, and was published in 1983. The protein is an inhibitor of trypsin, an enzyme whose role it is to break down other proteins. This protein includes six cysteines that oxidize to form three disulfide bonds. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!

1356: Revisiting Puzzle 92: Bacteria

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.

1355: 100 Residue Monomer Design: Helix Restrictions

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!

1354: Revisiting Puzzle 91: Virus Protein

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.

1353: Unsolved De-novo Freestyle 102

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!

1352: 90 Residue Monomer Design: Helix Restrictions

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!

1351: Revisiting Puzzle 90: Heliomicin

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.

1350: Unsolved De-novo Freestyle 101: Predicted Contacts

This is a follow-up puzzle for Puzzle 1347, now with Predicted Contacts to help guide your folding! See the blog for information on using the contact map. You can see the predicted contacts for this protein by clicking the Contact Map button in the Main menu (Selection Interface) or in the Actions tab (Classic Interface). You will notice that different contacts are shown in different shades of green, with brighter green contacts indicating stronger predictions. Players will be able to load in manual saves from Puzzles 1344 and 1347 and use them as a starting point here.

1349: 75 Residue Monomer Design: Helix Restrictions

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!

1348: Revisiting Puzzle 89 with Density: Cow Eye

This is a repost of Puzzle 1345, now with an electron density map! 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. Players may load in solutions from Puzzle 1345.