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Automated identification of functional dynamic contact networks from X-ray crystallography
Published Web Location
http://europepmc.org/articles/PMC3760795?pdf=renderNo data is associated with this publication.
Abstract
Protein function often depends on the exchange between conformational substates. Allosteric ligand binding or distal mutations can stabilize specific active-site conformations and consequently alter protein function. Observing alternative conformations at
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