Cover Picture: Allostery at a Protein‐Protein Interface Harboring an Intermolecular Motional Network (Angew. Chem. Int. Ed. 47/2024)

Dynamic networks are important devices for allosteric regulation of protein function. In their Communication (e202411472), Rasmus Linser and co‐workers use NMR spectroscopy and simulations to show that intermolecular association can make a connection for such networks to arise from segments previous...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2024-11, Vol.63 (47), p.n/a
Main Authors: Medina Gomez, Sara, Gonzalez, Tye I., Vasa, Suresh K., Linser, Rasmus
Format: Article
Language:English
Online Access:Get full text
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Summary:Dynamic networks are important devices for allosteric regulation of protein function. In their Communication (e202411472), Rasmus Linser and co‐workers use NMR spectroscopy and simulations to show that intermolecular association can make a connection for such networks to arise from segments previously bearing unrelated motion. Awareness of this kind of constructive, switchable modulation could help understanding and exploiting allosteric modulators for pharmacological or biotechnological avenues.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.202416799