Investigating the role of large-scale domain dynamics in protein-protein interactions

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

Research output: Contribution to journalShort surveypeer-review

18 Scopus citations


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.

Original languageEnglish
Article number54
JournalFrontiers in Molecular Biosciences
Issue numberSEP
StatePublished - 13 Sep 2016


  • 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


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