Laboratory evolution of protein conformational dynamics
•Laboratory directed evolution and ancestral reconstruction can facilitate study of protein structural dynamics.•Advances in biophysical and computational techniques facilitate this investigation.•Conformational dynamism is valuable in the acquisition of new function, as multiple potentially product...
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Published in | Current opinion in structural biology Vol. 50; pp. 49 - 57 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.06.2018
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Subjects | |
Online Access | Get full text |
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Summary: | •Laboratory directed evolution and ancestral reconstruction can facilitate study of protein structural dynamics.•Advances in biophysical and computational techniques facilitate this investigation.•Conformational dynamism is valuable in the acquisition of new function, as multiple potentially productive conformations can be sampled.•Evolution ‘freezes out’ unproductive motions, reducing unnecessary dynamics.
This review focuses on recent work that has begun to establish specific functional roles for protein conformational dynamics, specifically how the conformational landscapes that proteins can sample can evolve under laboratory based evolutionary selection. We discuss recent technical advances in computational and biophysical chemistry, which have provided us with new ways to dissect evolutionary processes. Finally, we offer some perspectives on the emerging view of conformational dynamics and evolution, and the challenges that we face in rationally engineering conformational dynamics. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
ISSN: | 0959-440X 1879-033X |
DOI: | 10.1016/j.sbi.2017.09.005 |