Foldit Puzzles

1803: Aflatoxin Challenge: Round 14 Loop Prediction

Refold the loops in this Aflatoxin Challenge design! After Round 13, where Foldit players redesigned the binding loops of an oxidation enzyme, the Siegel Lab found that some designs had high oxidative activity for other molecules--but no activity against aflatoxin! We think the redesigned loops might be misfolding when aflatoxin is not in the binding pocket. Misfolded loops could prevent the enzyme from binding aflatoxin and catalyzing the oxidation reaction. We wonder if Foldit players can predict how these binding loops might misfold, by refolding the loops in ways that score better than the original design! If we can figure out how the binding loops misfold, then we might be able to fix them and recover activity against aflatoxin!

1802: Sketchbook Symmetric Trimer Design: 70 Residues

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!

1801: Revisiting Puzzle 93: Spider Toxin

This is a throwback puzzle to the early days of Foldit. This small toxin is produced from the funnel-web spider A. aperta, and induces paralysis in insects by blocking calcium channels. This protein contains eight cysteines that oxidize to form four 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.

1800: Poly-Proline Helix Design: Round 9

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!

1799: Sketchbook Symmetric Trimer Design: 90 Residues

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!

1798: 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, and to provide newer players with easier puzzles that are still scientifically relevant.

1797: CRISPR-Cas Transposase Part II: Electron Density

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.

1796: Symmetric Trimer Design: 80 Residues

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!

1795: 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, and to provide newer players with easier puzzles that are still scientifically relevant.

1794: CRISPR-Cas Transposase Part I: Electron Density

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.