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

Front. Mol. Biosci.,
Front. Mol. Biosci., online article

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.

TU München
Helmholtz München
MPI of Neurobiology
MPI of Biochemistry