Foldit Puzzles

1452: Unsolved De-novo Freestyle 121

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!

1453: Sketchbook Puzzle - Splicing Factor

This protein is involved in transcription regulation and gene expression. It is also associated with both colorectal and liver cancer. In this experimental puzzle you will have 250 moves at your disposal. Once you use them up, you can reset and try something else!

1451: Splicing Factor

This protein is involved in transcription regulation and gene expression. It is also associated with both colorectal and liver cancer.

1449: Large Monomer Design

This puzzle challenges players to design a single-chain protein with 85-105 residues. We've softened the penalties associated with the Core Existence filter, which have typically been very steep. The starting structure has 85 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!

1448: Classroom Puzzle: Amyloid Protein

The misfolding and aggregation of amyloid proteins underlies many diseases, including Alzheimer’s disease, Parkinson’s disease, and ALS. However, the process by which protein misfolding causes cell toxicity and death is still heavily debated. In this puzzle, players are provided with three copies of the Aβ peptide, which forms amyloid fibrils in the brains of those afflicted with Alzheimer’s disease. In addition to amyloid fibrils, Aβ is known to form small soluble clusters. There is some evidence that these small clusters are more toxic than the amyloid fibrils, but the structure of such Aβ clusters is still unknown. In this puzzle, players can explore the different possibilities for how these small clusters of Aβ might fold.

1445: Aflatoxin Challenge: Round 2 with Insertions

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.

1447: Unsolved De-novo Freestyle 120

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!

1446: Y1 Receptor Ligand Docking

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.

1444: Unsolved De-novo Freestyle 119

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!

1443: Classroom Puzzle: Engineer the Active Site

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!