Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level.
Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level.
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在单分子水平上揭示溶液相本质无序 Tau 蛋白的构象变异。
DOI：
10.1002/anie.201708242
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发表时间：
2017
期刊：
影响因子：
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通讯作者：
Goldsmith,RandallH
中科院分区：
文献类型：
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作者：
Manger,LydiaH;Foote,AlexanderK;Wood,SharlaL;Holden,MichaelR;Heylman,KevinD;Margittai,Martin;Goldsmith,RandallH
内在无序的蛋白质，如tau蛋白，在溶液中采用多种构象，使溶液相结构研究复杂化。我们采用了一个反布朗电动（ABEL）陷阱来延长溶液中单个tau蛋白的测量时间。捕获后，我们记录了荧光各向异性，以研究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，而通过捕获球形蛋白或单个荧光团获得的分布则不是。时间分辨荧光各向异性测量用于解释双峰分布源于两个不同构象家族的压实位移。
Intrinsically disordered proteins, such as tau protein, adopt a variety of conformations in solution, complicating solution‐phase structural studies. We employed an anti‐Brownian electrokinetic (ABEL) trap to prolong measurements of single tau proteins in solution. Once trapped, we recorded the fluorescence anisotropy to investigate the diversity of conformations sampled by the single molecules. A 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. Time‐resolved fluorescence anisotropy measurements were used to provide an explanation of the bimodal distribution as originating from a shift in the compaction of the two different families of conformations.