Puzzles Feed

Closed

Puzzle
Expired: 09/05/18 18:00:00
1 comment
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 10,371
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This protein binds copper ions so that they may be transported safely to the cell compartments and enzymes that require them. 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.
Puzzle
Expired: 09/03/18 23:00:00
6 comments
Top Group: Anthropic Dreams
Top Player: fiendish_ghoul
Top Score: 18,773
Categories: Design, Overall, Symmetry
This symmetric design puzzle has C2 symmetry, with two symmetric chains. The H-bond Network Bonus encourages players to bury satisfied H-bond networks at the interface between the two chains. We've doubled the H-bond network bonus, but we'd like players to focus on building networks deep in the core of the protein complex. There are a couple other bonuses 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!
Puzzle
Expired: 08/30/18 23:00:00
1 comment
Top Group: Gargleblasters
Top Player: actiasluna
Top Score: 12,183
Categories: Design, Overall
This puzzle challenges players to design a single-chain protein with 65-75 residues. The starting structure has 65 residues, but more can be added at a cost of 32 points per residue. We've recently amended the old system of Conditions, or Filters. These have been rebranded as Objectives, and are reformulated so that they typically increase the base Foldit score (although it is still possible to receive a penalty from an Objective, in some cases). Ultimately, the function of each Objective is the same as it always has been (e.g. adding a residue still subtracts 32 points from the Residue Count objective), but we hope that the Objectives will be more encouraging than the old Filters—especially for new players who are still getting the hang of things. 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!
Puzzle
Expired: 08/29/18 18:00:00
1 comment
Top Group: Beta Folders
Top Player: LociOiling
Top Score: 9,868
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This storage protein is used to stockpile amino acids for future use, and is found at high concentration in the seeds of certain plants. This particular protein was used by scientists in 2011 to collect the highest-resolution crystal structure to date. This protein contains six cysteine residues that oxidize to form three disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
Puzzle
Expired: 08/27/18 23:00:00
2 comments
Top Group: Go Science
Top Player: NinjaGreg
Top Score: 14,300
Categories: Design, Overall
This puzzle is a little different from other H-bond network design puzzles in Foldit. This protein is another dimer (i.e. two chains fold up and bind each other) that was designed in the Baker Lab. The original design has three different H-bond networks that span the interface between the two chains, but we've mutated the network residues to alanine. In order to solve this puzzle, Foldit players will have to mutate the alanine residues back into residues that can form satisfied H-bond networks. The protein backbone is fixed in this puzzle, and only the alanine residues can be mutated. We want to know how well Foldit players are able to find networks using the tools currently in Foldit.
Puzzle
Expired: 08/23/18 23:00:00
3 comments
Top Group: Beta Folders
Top Player: matosfran
Top Score: 14,111
Categories: Design, Overall
This puzzle challenges players to design a single-chain protein with 95-120 residues. The starting structure has 95 residues, but more can be added at a cost of 32 points per residue. We've recently amended the old system of Conditions, or Filters. These have been rebranded as Objectives, and are reformulated so that they typically increase the base Foldit score (although it is still possible to receive a penalty from an Objective, in some cases). Ultimately, the function of each Objective is the same as it always has been (e.g. adding a residue still subtracts 32 points from the Residue Count objective), but we hope that the Objectives will be more encouraging than the old Filters—especially for new players who are still getting the hang of things. 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!
Puzzle
Expired: 08/22/18 18:00:00
1 comment
Top Group: Beta Folders
Top Player: matosfran
Top Score: 10,181
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This eelpout protein binds nucleated ice crystals to inhibit their growth. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
Puzzle
Expired: 08/20/18 23:00:00
1 comment
Top Group: Contenders
Top Player: Bletchley Park
Top Score: 16,664
Categories: Design, Overall, Symmetry
This symmetric design puzzle has C2 symmetry, with two symmetric chains. The H-bond Network Bonus encourages players to bury satisfied H-bond networks at the interface between the two chains. We've doubled the H-bond network bonus, but we'd like players to focus on building networks deep in the core of the protein complex. There are a couple other bonuses 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!
Puzzle
Expired: 08/16/18 23:00:00
5 comments
Top Group: Gargleblasters
Top Player: actiasluna
Top Score: 11,781
Categories:
This puzzle challenges players to design a single-chain protein with 75-90 residues. The starting structure has 75 residues, but more can be added at a cost of 32 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!
Puzzle
Expired: 08/15/18 18:00:00
1 comment
Top Group: Contenders
Top Player: georg137
Top Score: 9,991
Categories: Overall, Prediction
This is a throwback puzzle to the early days of Foldit. This small peptide was discovered in platypus venom—a rare instance of mammalian-produced venom, although this peptide appears similar to more widespread antimicrobials. This protein contains six cysteine residues that oxidize to form three disulfide bonds. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
Get Started: Download
  Windows    OSX    Linux  
Windows
(7/8/10)
OSX
(10.7 or later)
Linux
(64-bit)

Are you new to Foldit? Click here.

Are you a student? Click here.

Are you an educator? Click here.
Search
Only search fold.it
Recommend Foldit
User login
Soloists
Evolvers
Groups
Topics
Top New Users
Sitemap

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, Amazon, Microsoft, Adobe, RosettaCommons