Foldit Puzzles
Play puzzles to help scientific research and compete with other players. New puzzles are posted every week.
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The Crimean-Congo Hemorrhagic Fever (CCHF) is a life-threatening zoonotic disease caused by a tick-borne virus. Recent research has revealed the significant role of the viral-encoded Ovarian Tumor (OTU) deubiquitinase in the CCHFV replication process. Based on the most promising compounds, this puzzle will focus on getting an inhibitor for this protein. As the CCHFV-OTU protease interacts with another protein (ubiquitin), the interaction surface is quite large and superficial, making it a challenging binding pocket. For this round we will be focusing on the upper binding pocket. For more details check out the Crimean-Congo Hemorrhagic Fever blog post.
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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.
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This is a throwback puzzle to the early days of Foldit. This protein helps to maintain the reduction potential of the cell. The starting structure is a Rosetta model. This protein contains four cysteine residues, but only two of them oxidize to form a single disulfide bond. 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 problems that are still scientifically relevant.
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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 four copies of the same small protein, but not all the segments that are visible are the same.
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This is a throwback puzzle to the early days of Foldit. This domain is part of a T-cell receptor that recognizes pathogens in the body; the starting structure is a Rosetta model. This protein contains two cysteine residues which oxidize to form one disulfide bond. 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 problems that are still scientifically relevant.
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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. Note- the map here is really blobby!
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This is a throwback puzzle to the early days of Foldit. This pilin protein allows the P. aeruginosa bacterium to adhere to human cells, sometimes resulting in infection. The starting structure is a Rosetta model. This protein contains two cysteine residues which oxidize to form one disulfide bond. 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.
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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.