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Design a binder against coronavirus! This puzzle introduces a new objective: the Buried Unsats Objective detects "unsatisfied" polar atoms that cannot make hydrogen bonds with the water surrounding the protein. If your designed protein creates Buried Unsats, then it will be less likely to fold and bind to the coronavirus target. (Note that this target protein includes 8 buried unsats that players will be unable to fix.) See the blog for more details about buried unsats, and for helpful tips to make a successful protein binder! Players will be unable to load solutions from previous puzzles.

This is a throwback puzzle to the early days of Foldit. This protein is involved in the process of exocytosis, transporting proteins to the cell membrane or extracellular areas. The protein is modeled here in reduced form, 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 and to provide newer players with puzzles that are still scientifically relevant.

Fold this coronavirus protein! This is one portion of a larger protein encoded in the viral genome of SARS-CoV-2. It is encoded in a region of the genome called NSP2, but the protein's structure and function are still unknown. If we knew how this protein folds, we might be able to figure out its exact function. The puzzle's starting structure shows SS predictions from PSIPRED, and hints which parts of the protein might fold into helices or sheets. Refold this protein to find high-scoring solutions, which will tell us how this protein is most likely to fold!

Design an anti-inflammatory protein for COVID-19! The starting structure is a design by Bruno Kestemont from Puzzle 1824, as featured in our latest video Lab Report #8. Players may work to try and improve the starting structure, but also have the freedom to redesign binder from scratch. The best designs will have lots of helix or sheet structure, with a large core of orange hydrophobics. See our previous blog post for tips about designing a successful binder! Players may not load in solutions from previous puzzles.

Refold the loops in this Aflatoxin Challenge design! This is a followup to Round 15, this time starting with a completely unfolded loop. Previously, Foldit players had redesigned the binding loops of an oxidation enzyme, and testing at 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!

This is a throwback puzzle to the early days of Foldit. This toxin is produced in the intestines of the African black mamba. The protein contains ten cysteines 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 and to provide newer players with puzzles that are still scientifically relevant.

Design a binder against coronavirus! This puzzle is similar to Rounds 1 and 2 of our Coronavirus Binder Design challenge. but with tighter limits on the allowed number of segments. The starting structure has 177 segments, and players may use no more than 182 total. See the Foldit blog for tips on making a successful protein binder!

Note: This puzzle replaces Puzzle 1828, which had some errors in the protein backbone. Players may load solutions saved in Puzzle 1828.

This is a throwback puzzle to the early days of Foldit. This protein is an allergen produced by the white birch tree. 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 puzzles that are still scientifically relevant.

Refold the loops in this Aflatoxin Challenge design! This is a followup to Round 14, this time starting with a completely unfolded loop. Previously, Foldit players had redesigned the binding loops of an oxidation enzyme, and testing at 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!