Foldit Puzzles

1783: Revisiting Puzzle 87: Zinc Binding Protein

This is a throwback puzzle to the early days of Foldit. This small peptide is part of a larger protein that helps to regulate cell division, and is very important in early embryonic development. The protein is modeled here as in a reduced environment, so no disulfide bonds are expected to form. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1782: Symmetric Tetramer Design: H-bond Networks

Design a symmetric tetramer, with 4 identical chains that assemble together! 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.

1781: Poly-Proline Helix Design: Round 6

This is the sixth puzzle in the poly-proline helix design series! The starting structure is an 80 reside protein with a 5 residue helix, and all residues are mutable. However we have also increased the reference weight of proline from 16.4 to 50.0 to incentivize keeping proline part of the final design. There were some designs from the previous puzzle that satisfied a good fraction of the oxygens and nitrogens on the helix backbone, and we hope to see that continue. Hydrogen bonds are visible by selecting 'Show advanced GUI' in General Options in the Menu tab, and then selecting 'Show bonds (loop)' and 'Show bondable atoms' in the View tab.

1780: Revisiting Puzzle 86: Nematode

This is a throwback puzzle to the early days of Foldit. This protein, isolated from the hookworm A. caninum, is an extremely potent anticoagulant. This protein contains ten cysteine residues that oxidize to form five disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1779: Symmetric Tetramer Design: H-bond Networks

Design a symmetric tetramer, with 4 identical chains that assemble together! 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.

1778: Poly-Proline Helix Design: Round 5

This is the fifth puzzle in the poly-proline helix design series! We have shortened the helix to six residues while keeping the 80 residue protein that you are familiar with to make it easier to satisfy the polar atoms. All residues are mutable. We want satisfying the buried oxygens on the helix with hydrogen bonds to be a priority because if they are not, then the protein cannot fold. We hope to introduce a buried polars score filter soon to help you identify which residues are buried. Until then, hydrogen bonds are visible by selecting 'Show advanced GUI' in General Options in the Menu tab, and then selecting 'Show bonds (loop)' and 'Show bondable atoms' in the View tab.

1777: Revisiting Puzzle 85: Cell Adhesion Protein

This is a throwback puzzle to the early days of Foldit. This small domain is part of a larger protein that mediates interactions between other proteins in human development. This protein contains several cysteine residues, but we are modeling them in a reducing environment, so they should NOT form disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.

1776: Symmetric Tetramer Design: H-bond Networks

Design a symmetric tetramer, with 4 identical chains that assemble together. 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.

1775: Poly-Proline Helix Design: Round 4

This is the fourth puzzle in the poly-proline helix design series! The starting structure is identical to the one in round 3, with an 80 residue protein and an 8 residue helix. The backbone will be frozen to maintain the poly-proline helix secondary structure, but we are now giving you free rein to design the residues on the helix. We want to see how you will satisfy the exposed oxygens on the helix backbone, because proteins that satisfy all internal oxygens with hydrogen bonds have the best chance of folding in the lab.

1774: Revisiting Puzzle 84: Giant Anemone

This is a throwback puzzle to the early days of Foldit. This toxin, which is released by the sea anemone A. xanthogrammica, disrupts normal contraction of cardiac muscle in potential predators, and furthermore serves as a pheromone to signal danger to nearby anemones. 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.