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1003: Revisiting Puzzle 141: Rosetta Decoy 5

Closed since over 11 years ago

Intermediate Intermediate Intermediate Intermediate Intermediate Intermediate Overall Overall Overall Overall Overall Overall Prediction Prediction Prediction Prediction Prediction Prediction

Summary

Created
October 21, 2014
Expires
Max points
100
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.

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Comments

bkoep Staff Lv 1

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 Lv 1

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.