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Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5020063 | PMC |
| http://dx.doi.org/10.3389/fmolb.2016.00054 | DOI Listing |
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