1439: Classroom Puzzle: Chaperone Folding
|Name:||1439: Classroom Puzzle: Chaperone Folding|
|Expired:||10/17/2017 - 23:00|
|Description:||How chaperones help proteins to fold is still a matter of great debate in the scientific literature. This Classroom puzzle will help students explore different possible ways that a chaperone can interact with its client proteins. The puzzle includes a frozen chaperone protein—a miniaturized version of GroEL that can perform some of the functions of the full GroEL chaperone. The folding client is barnase, an well-behaved bacterial protein that is a popular model in protein folding studies. Players can choose to start with barnase in either the folded or unfolded state. To switch between the folded and unfolded starts, reset the puzzle (see the Actions menu in Original Interface; or the Undo menu in Selection Interface). It will be up to you to determine what provides the optimal balance between folding and interaction with the chaperone!
University of Denver students will be asked to read two articles alongside this Foldit puzzle. The first is a 1996 paper by Zahn et al., which reports chaperone activity in this small subdomain of the larger GroEL complex. The second is a 2008 study by Tang et al., in which the authors investigate GroEL function by testing the chaperone activity of GroEL mutants with different properties. See the blog for more information about the Classroom puzzle series.
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