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.
Highlights
Elise Delaforge 1, Sigrid Milles 1, Jie-rong Huang 1, Denis Bouvier 1, Malene Ringkjøbing Jensen 1, Michael Sattler 2, 3, Darren J
We describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular nuclear magnetic resonance (NMR) spectroscopy, are used to investigate conformational exchange on very different timescales
We will discuss the application of NMR, small-angle X-ray scattering (SAXS), and single molecule Förster resonance energy transfer (FRET) to the study of the conformational sampling of two highly flexible multi-domain proteins, the human U2AF65 protein that plays an essential role in the spliceosome assembly (Banerjee et al, 2003; Wahl et al, 2009; Mackereth et al, 2011), and the 627-nuclear localization signal (NLS) domain of the PB2 segment of influenza polymerase (Tarendeau et al, 2008; Delaforge et al, 2015)
Summary
Elise Delaforge 1, Sigrid Milles 1, Jie-rong Huang 1, Denis Bouvier 1, Malene Ringkjøbing Jensen 1, Michael Sattler 2, 3, Darren J. Disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function.
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