Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
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The structure of this protein has already been solved and published, but close inspection suggests that there are some problems with the published solution. We'd like to see if Foldit players can use the same electron density data to reconstruct a better model. This puzzle has two identical chains and some DNA, and comes from PDB entry 2H8R. It's a bit large, so the trim tool is recommended. Happy new year everyone!
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This is a throwback puzzle to the early days of Foldit. This DNA-binding domain is part of a bacterial integrase protein, which facilitates the insertion of new DNA into the bacterial chromosome. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
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NaV1.7 is a voltage-gated sodium channel that plays a key role in the generation and propagation of action potentials, especially in neurons involved in pain signaling. Genetic studies have revealed that loss-of-function mutations in NaV1.7 can result in congenital insensitivity to pain, while gain-of-function mutations are associated with severe, painful disorders. This makes NaV1.7 a promising therapeutic target for the development of non-addictive painkillers—a much-needed alternative to current opioid-based treatments.
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The structure of this protein has already been solved and published, but close inspection suggests that there are some problems with the published solution. We'd like to see if Foldit players can use the same electron density data to reconstruct a better model. This puzzle has two identical chains, and comes from PDB entry 2GFP. It's large, so the trim tool is recommended.
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This is a throwback puzzle to the early days of Foldit. This protein helps to transfer electrons between substrates in bacteria. The protein is modeled here in reducing conditions, and 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.
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NaV1.7 is a voltage-gated sodium channel that plays a key role in the generation and propagation of action potentials, especially in neurons involved in pain signaling. Genetic studies have revealed that loss-of-function mutations in NaV1.7 can result in congenital insensitivity to pain, while gain-of-function mutations are associated with severe, painful disorders. This makes NaV1.7 a promising therapeutic target for the development of non-addictive painkillers—a much-needed alternative to current opioid-based treatments.
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The structure of this protein has already been solved and published, but close inspection suggests that there are some problems with the published solution. We'd like to see if Foldit players can use the same electron density data to reconstruct a better model. This puzzle has two identical chains, and comes from PDB entry 2F7K. It's large, so the trim tool is recommended.
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This is a throwback puzzle to the early days of Foldit. This human protein helps to regulate the reduction potential of the cell, and should be modeled here in reduced form (with no 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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The structure of this protein has already been solved and published, but close inspection suggests that there are some problems with the published solution. We'd like to see if Foldit players can use the same electron density data to reconstruct a better model. This puzzle has three chains, and comes from PDB entry 2EQB.
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This is a throwback puzzle to the early days of Foldit. This spinach protein is critical for photosynthesis, and participates in the electron transfer chain within the chloroplast. The protein is modeled here in the reduced state, 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.