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

本研究的目的是通过核磁共振技术研究透析相关性淀粉样变性中β2-微球蛋白（β 2 m）的构象变化。据信β 2 m通过部分结构化状态形成淀粉样蛋白原纤维。然而，从目前的数据来看，我们认为部分结构化状态应该被“激活”为广泛的未折叠状态，其中疏水残基暴露以与种子缔合。

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.