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Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

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Delaforge, Elise | Milles, Sigrid | Huang, Jie-Rong | Bouvier, Denis | Jensen, Malene Ringkjøbing | Sattler, Michael | Hart, Darren J | Blackledge, Martin

Edité par CCSD ; Frontiers Media -

International audience. Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.

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