Molten globule precursor states are conformationally correlated to amyloid fibrils of human β-2-microglobulin.
作者： Lukasz Skora , Stefan Becker , Markus Zweckstetter
DOI: 10.1021/JA100453E
关键词:
摘要: Misfolding intermediates play a key role in defining aberrant protein aggregation and amyloid formation more than 15 different human diseases. However, their experimental characterization is challenging due to the transient nature conformational heterogeneity of involved states. Here, we demonstrate that direct carbon-detected NMR experiments allow observation, assignment, structural analysis molten globule are severely broadened by exchange. The method used characterize structure dynamics partially unfolded 99-residue beta-2-microglobulin, which major component insoluble aggregates occurring dialysis-related amyloidosis. Comparison properties globule-like with levels deuterium incorporation into fibrils beta-2-microglobulin revealed close relationship between metastable beta-sheet-rich beta-2-microglobulin.
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