An anti-Brownian electrokinetic trap was employed to prolong measurements of single tau proteins in solution. Once trapped, the fluorescence anisotropy was recorded to investigate the diversity of conformations sampled by the single molecules. The distribution of anisotropy values obtained from trapped tau protein is conspicuously bimodal while those obtained by trapping a globular protein or individual fluorophores are not.

中文翻译：

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在单分子水平上揭示溶液相本征紊乱的Tau蛋白的构象变异。

使用抗布朗电动势阱来延长溶液中单个tau蛋白的测量时间。一旦被捕获，就记录荧光各向异性，以研究由单个分子采样的构象的多样性。从捕获的tau蛋白获得的各向异性值的分布明显是双峰的，而通过捕获球状蛋白或单个荧光团获得的各向异性值的分布却不是。