New Foldon Symmetry puzzles
Foldon is a small, 27 residue domain from the C-terminus of a phage virus protein called fibritin. It functions to ensure trimerization and proper folding of the rest of the fibritin domain, but it folds just as capably in isolation. Biophysicists have taken note of its remarkable stability and propensity for trimerization, and have successfully fused foldon to other domains, forming a number of engineered trimeric proteins.
Your job, in this puzzle, is to take an opposite approach. Instead of attaching three copies of a known domain to foldon in order to form a trimer, you’ll be given twenty extra residues extending from foldon’s
N-terminus and asked to fold these chains into a larger trimeric domain that includes foldon. You’ll be allowed to move foldon around as well, but you can only mutate the residues in the polyalanine extension. And remember, three-fold symmetry will be enforced!
Our hope is to synthesize one of your best-scoring structures, in an attempt to generate (via NMR or X-ray crystallography) an experimental structure!
We’ll be using foldon, and some of the larger trimer domains that you generate, in our efforts to make higher-order assemblies: rigid crystals, capsules, and nanowires.
( Posted by
beta_helix 182 4086 |
Wed, 12/07/2011 - 00:38 |
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The Carver College of Medicine at the University of Iowa needs your help!
After the most recent Foldit paper came out, our lab was contacted by scientists at University of Iowa Carver College of Medicine working on a currently unsolved transcription factor. Their Department of Internal Medicine hopes you can help them with this protein, here is their message to you:
"The Foldit group has recently demonstrated that focused play can achieve results that have eluded structural biologists for over a decade. Congratulations on your efforts! Our next set of puzzles focuses on another significant real-world problem that has tremendous potential for curing a wide range of diseases using stem cell therapy.
Pluripotency is a unique biological property that characterizes rare stem cells during early development. Pluripotent stem cells can become any cell of the body and therefore have great potential for regenerative medicine. Nanog is one of three proteins that are essential for being able to convert or ‘reprogram’ skin cells into a pluripotent state. Solving this protein structure will help us design drugs that can activate this protein and its binding partners as a strategy for patient-specific tissue regeneration."
Try out puzzle 476: Unsolved Nanog Transcription Factor.
http://fold.it/portal/node/991002
beta_helix 182 4086 |
Fri, 11/04/2011 - 05:33 |
1 comment
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Latest Foldit paper named "Article of the month" by Nature Structural & Molecular Biology
The recent Nature Structural & Molecular Biology Foldit paper is their "Article of the month" which also means everyone has Free Access to the paper on the Nature website:
http://www.nature.com/nsmb/index.html
Just click on the *FREE ACCESS* button and you can read the paper, download the full size images and the Supplemental Material (at the bottom).
Congrats everyone!
( Posted by beta_helix 182 4086 |
Fri, 10/14/2011 - 19:33 |
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New Player Statistics
Again, welcome to all the new players that have recently joined Foldit and thank you to all the veteran Foldit players who have been helping everybody out!
It seems like the swell of new players has slowly gone down. Some players were asking how big that wave of new users was, so we wanted to show you the stats:
and you can compare these numbers to last month:
We also want to let all the new players know that even when you are not playing Foldit you can still help us fold proteins to fight diseases by installing Rosetta@home:
http://boinc.bakerlab.org/rosetta/
By running the Rosetta program on your computer while you don't need it you will help us speed up and extend our research in ways we couldn't possibly attempt without your help. We often post Rosetta models outputted from Rosetta@home as Foldit puzzles.
beta_helix 182 4086 |
Sat, 10/01/2011 - 00:00 |
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Link to the new Foldit Nature article
We posted the just published NSMB paper. here it is:
http://www.cs.washington.edu/homes/zoran/NSMBfoldit-2011.pdf
This is the second Nature paper we published with Foldit discoveries. This is truly amazing accomplishment. All Foldit players should be proud.
We also have two more in the pipeline one of the algorithmic discoveries in Foldit recipes, and a brand new synthetic protein discovered primarily due to the insight of Foldit protein design. Stay tuned.
( Posted by zoran 182 14078 |
Sun, 09/18/2011 - 20:44 |
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