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

Elise Delaforge (1) , Sigrid Milles (1) , Jie-Rong Huang (1) , Denis Bouvier (1) , Malene Ringkjøbing Jensen (1) , Michael Sattler (2) , Darren J Hart (1) , Martin Blackledge (1)

1 IBS - UMR 5075 - Institut de biologie structurale
2 Institute of Structural Biology

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.

Mots clés: chemical exchange saturation transfer (CEST); conformational dynamics; free-energy landscape; multi-domain proteins; nuclear magnetic resonance (NMR); single molecule Förster resonance energy transfer (FRET); small angle scattering

Domaines: Biologie structurale [q-bio.BM]

Elise Delaforge, Sigrid Milles, Jie-Rong Huang, Denis Bouvier, Malene Ringkjøbing Jensen, et al.. Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions. Frontiers in Molecular Biosciences, 2016, 3, pp.54. ⟨10.3389/fmolb.2016.00054⟩. ⟨hal-01426889⟩