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Puzzle
Expired: 11/13/17 23:00:00
Top Group: Anthropic Dreams
Top Player: Galaxie
Top Score: 10,116
Categories: Overall, Prediction
The structure of this protein is still unknown. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!
Puzzle
Expired: 11/08/17 23:00:00
13 comments
Top Group: Go Science
Top Player: Bruno Kestemont
Top Score: 13,658
Categories: Overall
This is a follow-on puzzle of Puzzle 1441: Y1 Receptor Homology Modeling. In the previous puzzle, we asked you to model the structure of the human Y1 neuropeptide receptor. In this puzzle, we'd like you to determine how a known binder of Y1 interacts with that model.

Puzzle
Expired: 11/14/17 23:00:00
10 comments
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 16,074
Categories: Design, Overall
Aflatoxins are a class of poisonous compounds that contaminate a significant portion of the global food supply. In this puzzle, players are challenged to redesign an enzyme that could break down aflatoxin molecules. The majority of the protein is frozen, with the aflatoxin ligand fixed in a binding pocket. Surrounding the binding pocket are a number of loops that might be redesigned without affecting the folding stability of the protein. In these loops, players may manipulate the protein backbone and mutate the residue sidechains. Players may add up to 20 additional residues within these loops, at a cost of 16 points per residue. Players may load in solutions from Puzzle 1440.
Puzzle
Expired: 11/06/17 23:00:00
1 comment
Top Group: Go Science
Top Player: ZeroLeak7
Top Score: 10,147
Categories: Overall, Prediction
The structure of this protein is still unknown. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!
Puzzle
Expired: 11/01/17 23:00:00
3 comments
Top Group: Anthropic Dreams
Top Player: Galaxie
Top Score: 9,656
Categories: Experimental
How enzymes catalyze reactions is still an ongoing debate in the biochemistry literature. Some people think it's most important that the active site provides the right chemical environment, others that the geometry be perfected, and others that think that the motions of the protein are most important. This puzzle is meant to allow you to try and design the active site to make the best possible enzyme. One way to improve an enzyme's activity is by binding the transition state of the reaction tighter. In this puzzle, we've put a transition-state analog into the active site, and would like you to try and improve the binding to that analog by redesigning the active site residues!
Puzzle
Expired: 10/27/17 18:00:00
Top Group: Go Science
Top Player: Hollinas
Top Score: 8,645
Categories: Experimental
This small protein interferes with cellular adhesion and, consequently, clotting mechanisms. In this experimental puzzle you will have 250 moves at your disposal. Once you use them up, you can reset and try something else!
Puzzle
Expired: 10/24/17 23:00:00
7 comments
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 10,444
Categories: Overall, Prediction
The neuropeptide Y receptors are a group of human cell surface receptors found in the brain and digestive system, and are involved in regulating hunger and satiety. A better understanding of the neuropeptide Y receptors could allow scientists to better understand the diseases and disorders which involve misregulation of hunger and satiety. Treatment of obesity is the obvious example, but there are other disorders characterized by a mis-regulation of hunger (such as Prader-Willi syndrome). Chemotherapy is often associated with appetite suppression, so a treatment which can increase hunger could help reduce the dangerous weight loss sometimes seen in chemotherapy patients.
Puzzle
Expired: 10/31/17 23:00:00
26 comments
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 16,065
Categories: Design, Overall
Aflatoxins are a class of poisonous compounds that contaminate a significant portion of the global food supply. In this puzzle, players are challenged to redesign an enzyme that could break down aflatoxin molecules. The majority of the protein is frozen, with the aflatoxin ligand fixed in a binding pocket. Surrounding the binding pocket are a number of loops that might be redesigned without affecting the folding stability of the protein. In these loops, players may manipulate the protein backbone and mutate the residue sidechains. Redesign the loops of this protein to better bind the aflatoxin ligand!
Puzzle
Expired: 10/17/17 23:00:00
6 comments
Top Group: Contenders
Top Player: Bletchley Park
Top Score: 10,469
Categories: Experimental
How chaperones help proteins to fold is still a matter of great debate in the scientific literature. This Classroom puzzle will help students explore different possible ways that a chaperone can interact with its client proteins. The puzzle includes a frozen chaperone protein—a miniaturized version of GroEL that can perform some of the functions of the full GroEL chaperone. The folding client is barnase, an well-behaved bacterial protein that is a popular model in protein folding studies. Players can choose to start with barnase in either the folded or unfolded state. To switch between the folded and unfolded starts, reset the puzzle (see the Actions menu in Original Interface; or the Undo menu in Selection Interface). It will be up to you to determine what provides the optimal balance between folding and interaction with the chaperone!
Puzzle
Expired: 10/13/17 23:00:00
1 comment
Top Group: Anthropic Dreams
Top Player: markm457
Top Score: 10,225
Categories: Design, Overall
This puzzle challenges players to design a single-chain protein with 65-75 residues. We've softened the penalties associated with the Core Existence filter, which have typically been very steep. The starting structure has 65 residues, but more can be added at a cost of 16 points per residue. See the puzzle comments for filter 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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Developed by: UW Center for Game Science, UW Institute for Protein Design, Northeastern University, Vanderbilt University Meiler Lab, UC Davis
Supported by: DARPA, NSF, NIH, HHMI, Microsoft, Adobe, RosettaCommons