Foldit Puzzles

888: CASP11 Target T0763: Server Models

This CASP11 target has 163 residues, and we've provided you with 5 Robetta server models. Restart the puzzle to cycle through the alternate starting structures. See the puzzle comments for secondary structure predictions!

889: CASP11 Target T0769: Server Model

This CASP11 target has 106 residues, and the Robetta server has converged on a single structure. We've provided the Robetta prediction as the starting model, but feel free to explore other structures! See the puzzle comments for secondary structure predictions.

890: CASP11 T0759: WeFold Round (CLOSED and reposted as 890b)

This puzzle has been replaced by Puzzle 890b where you will be able to load in solutions from this puzzle. This puzzle will close in the next 24 hours...

887: 70 Residue Monomer Design: Strand Constrained

This is a single-chain design puzzle with 70 residues, and four of the residues are pre-folded into beta-strand conformation. These residues are somewhat flexible, but there are strong constraints to keep them close to beta-strand conformation. There are 3 filters enabled on this puzzle: the Residue IE Score monitors that all PHE, TYR, and TRP residues are scoring well; the Core Existence filter checks that at least 25% of the residues are buried in the core of your design; and the Fragment filter scans for parts of your design that are unlikely to fold up naturally. 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 3 designs that you want us to look at, even if they are not the best-scoring solutions!

886: CASP11 Target T0759: Server Models

This is the first CASP11 Foldit puzzle! This puzzle has 101 residues, and we've provided you with 5 Robetta server models (all generated from the same homology template). Restart the puzzle to cycle through the alternate starting structures.

885: De-novo Freestyle 39: Predicted Contacts

This is a follow-up puzzle for Puzzle 881, now with Predicted Contacts to help guide your folding. See the blog for information on the new contact map format! 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. High Wiggle Power has been disabled in this puzzle. Note that players will NOT be able to load in solutions from Puzzle 881.

884: 74 Residue Ebola Binder Design

This is a design puzzle similar to Puzzle 879—now with 74 residues—near the interface of a target glycoprotein from the Ebola virus. At the binding site of the Ebola protein, there is already a helix designed by scientists in the Baker Lab, but the helix will not fold up by itself! Build a scaffold around the starting design that will fold up properly and stabilize the binding helix! There are strong constraints to keep the binding helix in place, and you may not mutate residues at the interface. You may not add additional residues to the design, but you may delete residues from one end of the design and reinsert them at the other end. This puzzle includes a Residue IE Score filter and a Core Existence filter, and High Wiggle Power has been disabled. Remember to share your favorite designs using the Share with Scientist tool, even if those are not your best-scoring solutions!

884b: 74 Residue Ebola Binder Design

NOTE: This puzzle replaces Puzzle 884, which had scoring and filter calibration issues. Players may load in solutions from the originally posted puzzle.

883: De-novo Freestyle 38: Predicted Contacts

This is a follow-up puzzle for Puzzles 876 and 880, now with Predicted Contacts to help guide your folding. See the blog for information on the new contact map format! 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. For this puzzle, you will be able to load in previous solutions from Puzzles 876 and 880.

881: De-novo Freestyle 39: Low Power

In this de-novo freestyle puzzle, the "High Wiggle Power" option has been disabled. The results from these puzzles will help us determine how useful the wiggle power options may be for structure prediction in Foldit. The secondary structure predictions are provided on the starting model, with more details posted in the puzzle comments.