Abstract
The design of artificial enzymes has been a goal of many investigations for decades. This effort has not been successful. Not only are the vast majority of such designs inactive, but there is also no clear way to distinguish between the completely inactive designs and those showing a some amount of activity. If the concept of “transition state stabilization” was fully descriptive of the catalytic process, then the highly developed ability to design transition state complementary proteins should have borne some fruit. This talk will focus on one aspect of this challenging problem, the absence of rapid protein dynamics in many such structures. This difficulty has been made apparent through the study of laboratory evolved species of artificial enzymes. We will show how directed evolution, which is obviously completely agnostic when it comes to protein dynamics, builds this into some artificial enzymes, how this is accomplished, and what we can learn about de novo design.
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