1443: Classroom Puzzle: Engineer the Active Site
|Name:||1443: Classroom Puzzle: Engineer the Active Site|
|Expired:||11/01/2017 - 23:00|
|Description:||How enzymes catalyze reactions is still an ongoing debate in the biochemistry literature. Some people think it's most important that the active site provides the right chemical environment, others that the geometry be perfected, and others that think that the motions of the protein are most important. This puzzle is meant to allow you to try and design the active site to make the best possible enzyme. One way to improve an enzyme's activity is by binding the transition state of the reaction tighter. In this puzzle, we've put a transition-state analog into the active site, and would like you to try and improve the binding to that analog by redesigning the active site residues!
University of Denver students will be asked to read two articles alongside this Foldit puzzle. The first is a 1998 paper by Lau et al., who report computer simulations that suggest this enzyme relies on dynamic protein motions to enable the reaction. (Unfortunately this paper may not be freely available to all Foldit players.) A second, more recent, paper by Lameira et al. proposes an alternative mechanism that does not require on protein motions, but only a precisely organized active site.
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