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1003: Revisiting Puzzle 141: Rosetta Decoy 5
Status: Closed

Summary

Name: 1003: Revisiting Puzzle 141: Rosetta Decoy 5
Status: Closed
Created: 10/21/2014
Points: 100
Expired: 10/30/2014 - 23:00
Difficulty: Intermediate
Description: This is a throwback puzzle to the early days of Foldit. This protein helps to regulate oxidation in the cell; the starting structure is a model produced by Rosetta. We are revisiting old Foldit puzzles so we can see how useful the recent additions to the game have been.
Categories: Overall, Prediction

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Comments

brow42's picture
User offline. Last seen 5 days 11 hours ago. Offline
Joined: 09/19/2011
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almost adjacent cysteines

Is it common for bridges to from between cysteines that are this close?

bkoep's picture
User offline. Last seen 1 hour 20 sec ago. Offline
Joined: 11/15/2012
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Good question!

Not necessarily. In general, cysteines that are far apart in sequence can contribute more to the stability of a protein fold.

Since these two cysteines are so close in sequence, we can assume that this disulfide bond contributes very little to the stability of the protein. This makes sense, if we consider that this protein is involved in regulating the reduction potential of the cell: In order for the protein to function, the disulfide should be readily oxidized (formed) or reduced (broken) in response to changing conditions in the cell. This particular protein must remain folded even when the disulfide bond is reduced, so that the two cysteines are properly positioned and ready to bond.

brow42's picture
User offline. Last seen 5 days 11 hours ago. Offline
Joined: 09/19/2011
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Redox buffer

I see! So, this is a redox potential buffer, analogous to a pH buffer! Thank you for the response!

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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