Fig. 6. Model of β₂m amyloid fibril formation whereby WT β₂m unfolds at low pH and forms dynamic oligomers that reach a critical nucleus and then convert rapidly into mature amyloid fibrils. In the case of H51A, the point mutation causes oligomers to form rapidly, although these more abundant, highly populated and kinetically stable oligomers are significantly more stable and less dynamic than the WT β₂m oligomers and thus slower at converting into the critical nucleus that results in an increased lag-time of amyloid fibril formation.