Dataset associated with 'The effect of mutation on an aggregation-prone protein: An in vivo, in vitro and in silico analysis'

Aggregation of initially stably structured proteins is involved in more than 20 human amyloid diseases. Despite intense research, however, how this class of proteins assembles into amyloid fibrils remains poorly understood. We address this question using β2-microglobulin (β2m) as a model system, focusing on D76N-β2m that is involved in hereditary amyloidosis. Here, we identify the residues key to protect β2m from aggregation and we show that residue 76 has a unique ability to drive β2m aggregation in vivo and in vitro.