New Update: Symmetry!

We've just released an update which introduces a new concept to Foldit: Symmetry!

Symmetry in proteins refers to what we call oligomers: proteins that use many identical copies of themselves to bind together and form a "symmetric" complex. We call it symmetry because each copy folds the exact same way, and these copies arrange themselves with rotational or translational symmetry.

In the past, Foldit has only been capable of handling what we call monomers, which are not symmetric. With this update, we'll be able to have puzzles on a whole new array of structures (as it turns out, most proteins are symmetric!). Symmetric structures are also central to the design of nano-materials, and we'll be posting design puzzles to take advantage of this. The best part is, many of these proteins are small, and can be handled by Foldit.

Symmetry in Foldit works like this: you have one copy of the protein that you work on. This is called the independent unit. Around this copy, there are many other 'locked' copies that are symmetric. When you change the independent unit, the other copies will change themselves too. The goal is still to maximize your score, but now you are scored on two things: both how well the protein itself forms, and how well it interfaces with itself.

(Thu, 11/10/2011 - 02:00  |  2 comments)
steveB's picture
User offline. Last seen 2 years 48 weeks ago. Offline
Joined: 01/08/2009
Groups: Void Crushers
Align to guide

If you load in a solution as a guide on this puzzle, and then press 'G' to align to the guide, the guide moves around on each subsequent press of the button, and more importantly the 2 guide puzzle sections seprate from one another, eventually dissapearing into cyber space never to be seen again.

ipatrol's picture
User offline. Last seen 6 years 4 weeks ago. Offline
Joined: 12/04/2010
Groups: None
Ah, now you're adding

Ah, now you're adding quaternary structure to the mix. Nice touch. You should also add support for porphyrine structures, like heme groups. That should be all you need to finish a protein.

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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, Amazon, Microsoft, Adobe, RosettaCommons