NMR investigations of metal interactions with unstructured soluble protein domains.

Highlights: [•] Recent NMR findings on metal interactions with disordered protein domains are discussed. [•] Flexible domains derived either from amyloidogenic proteins or from metal chaperones are considered. [•] The NMR behaviors of different transition metal ions are discussed and compared. [•] The use of NMR to determine (i) the metal coordination sphere, (ii) the structure, (iii) the dynamics and (iv) the binding affinity is discussed. [•] All the benefits and drawbacks of the NMR method are addressed as well. [ABSTRACT FROM AUTHOR]