Bruno Kestemont Lv 1
When loading an old 1649 puzzle, we get our points but the 2 dimers are merged. Then on first action, the points turn (logically) to -999999999. The game is then to try to assemble the 2 dimers.
1652: Unsolved De-novo Freestyle 149: Symmetric Dimer
Closed since almost 7 years ago
Intermediate Overall Prediction SymmetrySummary
- Created
- March 21, 2019
- Expires
- Max points
- 100
This is a follow-up to Puzzle 1649: De-novo Freestyle 149, now with C2 symmetry. This protein was originally designed by a Foldit player as a symmetric dimer. In Puzzle 1649, we challenged the Foldit community to try and predict how the design might fold as a single, monomeric chain. Now we want to see if Foldit players can predict how the original protein was designed to fold and bind to itself with C2 symmetry. Players may load in solutions from Puzzle 1649. Secondary structure predictions (from PSIPRED) are marked on the starting structure, and provide clues about where the protein might form helices and sheets!
Sequence:
TEVLYLKDADVEQVVRYIRQKNAEVLVVVVNFDEEQIRIIVRVVIQIVQAEVVIVVINMEEEQVKKVVNQVNVKVVVVIK
Top groups
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100 pts. 14,722
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1. fiendish_ghoul Lv 1100 pts. 15,655
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Comments
NinjaGreg Lv 1
… just use the move tool before doing anything else, you can pull them apart intact.
frood66 Lv 1
Just a shame that we were not given this puzzle info when we played the monomer.
Ir was pretty clear that it was a player design - but knowing it was a dimer might have helped.
bkoep Staff Lv 1
I take this to mean that, "knowing it was a dimer might have helped [to predict it as a dimer]." I'm glad you brought this up, because it opens a discussion about the purpose of these puzzles, which may not be clear from the puzzle description.
In fact, we don't know this protein sequence actually forms a dimer—we only know that it was designed to form a dimer. The goal of these De-novo Freestyle puzzles is to look for decoy folds, or other ways the design sequence might fold up (i.e. ways that the design might fail). If Foldit players can find a high-scoring fold that is a monomer, that would suggest that the design is more likely to fold up as a monomer instead of the intended dimer.
For our purposes, we actually want to avoid biasing players towards the intended design. This is why we don't share the designed fold (or even the fact that it was designed as a dimer).
Skippysk8s Lv 1
clearly none of us managed to decoy this one. Well done