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

ABSTRACT: 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.

SUBMITTER: Delaforge E

PROVIDER: S-EPMC5020063 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

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

Delaforge Elise E Milles Sigrid S Huang Jie-Rong JR Bouvier Denis D Jensen Malene Ringkjøbing MR Sattler Michael M Hart Darren J DJ Blackledge Martin M

Frontiers in molecular biosciences 20160913

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 spectroscop ...[more]

PMID: 27679800

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