Foldit Puzzles

1557: Extra Small Monomer Design

This puzzle challenges players to design a single-chain protein with 60-65 residues. The starting structure has 60 residues, but more can be inserted at a cost of 32 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!

1556: Revisiting Puzzle 73: Polycystein

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.

1555: Find the Hydrogen Bond Networks: Round 2

This is a followup to Puzzle 1552, where we challenged players to find two H-bond networks, starting from two extended chains. In this puzzle, both chains are already folded at the start, but players will still need to dock the two chains together and arrange the interface to find the H-bond networks. This protein is a dimer (i.e. two chains fold up and bind each other) that was designed in the Baker Lab, with two identical H-bond networks that span the interface between the two chains. See if you can find the H-bond networks!

1554: Cryo-EM Multi-Start Puzzle

This protein is part of a large protein complex with multiple subunits, which has recently been the target of some cryo-electron microscopy (cryo-EM) experiments. We are giving you 5 different server predictions as starting points. Reset the puzzle to cycle through the different starting models. Try to look at where the different models agree and focus on the regions where the models vary!

1553: Sketchbook Puzzle - Revisiting Puzzle 62: Halorhodopsin

This protein is able to absorb light and use the energy to transfer chloride ions across the cell membrane. In this experimental puzzle you will have 256 moves at your disposal. Once you use them up, you can reset and try something else!

1550: Aflatoxin Challenge: Round 10

Redesign the active site to bind aflatoxin! This puzzle is much like Round 9 of the Aflatoxin Challenge, but now players may insert up to 20 extra residues into the designable loops, at a cost of 20 points per residue. Strong constraints will keep aflatoxin from moving too far from its starting position, but we think the extra wiggle room will allow Foldit players to design an active site that binds the molecule more tightly. 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.

1552: Find the Hydrogen Bond Networks!

This puzzle is a little different from other prediction puzzles in Foldit. This protein is a dimer (i.e. two chains fold up and bind each other) that was designed in the Baker Lab. The design has two identical H-bond networks that span the interface between the two chains. In order to solve this puzzle, Foldit players will have to fold each of the two chains, bring them together, and arrange the interface to form the two H-bond networks. The secondary structure of the designed protein is marked on the starting structure. See if you can fold this protein and find the H-bond networks!

1551: Sketchbook Puzzle - Revisiting Puzzle 68: Bos Taurus

This cow protein, found in epithelial cells of the intestine, binds calcium as it moves from the digestive tract into the blood. In this experimental puzzle you will have 128 moves at your disposal. Once you use them up, you can reset and try something else!

1549: Sketchbook Puzzle - Revisiting Puzzle 69: Scorpion Toxin

This is another potent neurotoxin produced by scorpions, similar to that found in Puzzle 1542b. This protein contains eight cysteine residues that oxidize to form four disulfide bonds. In this experimental puzzle you will have 256 moves at your disposal. Once you use them up, you can reset and try something else!

1548: Unsolved De-novo Freestyle 136

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!