Characterization of the transient intermediate of the β2-microglobulin amyloid fibril using solution NMR techniques

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The purpose of this study is to clarify how β2-Microglobulin (β2m), associated with the dialysis-related amyloidosis, changes its conformation when the disease develops by using nuclear magnetic resonance. It has been believed that β2m forms amyloid fibril through a partially structured state. However, from the present data, we suggested that the partially structured state should be "activated" to be extensively unfolded state, in which the hydrophobic residues are exposed to associate with the seed.