Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
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This is the same target that players folded in 1051: Symmetric De-novo Freestyle 48, now with electron density! The two chains are not constrained by symmetry in this puzzle, although we still expect them to adopt mostly-symmetric folds. The starting model is a solution built with an automated method—see if you can improve it! Players will not be able to load in solutions from Puzzle 1051.
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Design a binding pocket for vancomycin! Antibiotic resistance is an increasing problem and one of the last resorts for treating inflammation is the cyclic peptide vancomycin. Hence there is a general interest to generate proteins that can bind vancomycin and upon binding generate a signal. With this technology it would be possible to test patients that have been treated with antibiotics if they still have small amounts left before they leave e.g. a hospital. The aim of this puzzle is to optimize the interaction between a protein and the small molecule vancomycin.
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This is a throwback puzzle to the early days of Foldit. This protein binds fatty acids in intestinal cells. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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This puzzle again uses separate "Core Existence" filters for the monomer unit and the symmetric complex. Click the "Show" checkbox beneath the Core Existence filter to see which residues have been identified as Core (orange), Boundary (green), or Surface (blue). There are several other filters in effect; see the puzzle comments for 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!
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This is a symmetric dimer that was recently designed by Baker Lab scientists. See if you can find the correct fold! The secondary structure predictions are provided on the starting model, with more details posted in the puzzle comments.
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This is a throwback puzzle to the early days of Foldit. This small, intracellular domain binds to the CD2 T cell receptor (TCR), and plays a critical role in T cell activation during the immune response. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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This is a repost of Puzzle 1045, now with normal density scoring. Load in your solutions from Puzzle 1045 and see if you can improve them to fit the density! This is a small domain of the VipB protein, which is a component of the type VI secretion system in V. cholerae. NOTE: If you did not manually save a solution in Puzzle 1045, you can go back to 1045, manually save it, and the solution should appear in your manual saves for this puzzle.
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This puzzle is aimed at designing short peptides that fold into stable structures. We encourage the use of multiple disulfide bonds, but discourage GLY residues, which will score especially poorly here. See the puzzle comments for more information about filters. The Baker lab will run folding predictions on your best designs, and the the ones that perform well will be synthesized and further validated for structural stability. 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!
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This is a throwback puzzle to the early days of Foldit. These are the two chains of a bio-engineered variant of human insulin, which together complete three disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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This is a puzzle where you can redesign part of a player-designed protein. This is a monomer designed by viosca for Puzzle 1024: 75 Residue Monomer Design: Zero Cysteines. Our analysis shows that most of this protein is likely to fold, but that the first strand and loop can adopt some alternative conformations. Help us redesign this region of the protein to lock down the position of the first strand! Players may make mutations only at certain positions that contact the first strand. Players may also insert two additional residues in this region, but beware that changing the shape of the protein too much will disqualify your design!