Metal interactions of ?-synuclein probed by NMR amide-proton exchange
 

Metal interactions of ?-synuclein probed by NMR amide-proton exchange

The aberrant aggregation of ?-synuclein (?S), a disordered protein primarily expressed in neuronal cells, is strongly associated with the underlying mechanisms of Parkinson's disease. It is now established that ?S has a weak affinity for metal ions and that these interactions alter its conformational properties by generally promoting self-assembly into amyloids. Here, we characterised the nature of the conformational changes associated with metal binding by ?S using nuclear magnetic resonance...

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