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Advances in ion mobility spectrometry–mass spectrometry reveal key insights into amyloid assembly

机译:离子迁移谱-质谱的进展揭示了淀粉样蛋白组装的关键见解

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摘要

Interfacing ion mobility spectrometry to mass spectrometry (IMS–MS) has enabled mass spectrometric analyses to extend into an extra dimension, providing unrivalled separation and structural characterization of lowly populated species in heterogeneous mixtures. One biological system that has benefitted significantly from such advances is that of amyloid formation. Using IMS–MS, progress has been made into identifying transiently populated monomeric and oligomeric species for a number of different amyloid systems and has led to an enhanced understanding of the mechanism by which small molecules modulate amyloid formation. This review highlights recent advances in this field, which have been accelerated by the commercial availability of IMS–MS instruments. This article is part of a Special Issue entitled: Mass spectrometry in structural biology.
机译:离子淌度质谱与质谱(IMS-MS)的接口使质谱分析扩展到一个额外的维度,从而提供了无与伦比的分离和异质混合物中人口稀少物种的结构特征。从此类进展中受益匪浅的一种生物系统是淀粉样蛋白的形成。使用IMS-MS,在鉴定许多不同淀粉样蛋白系统的瞬时组装的单体和寡聚物种方面已取得进展,并导致人们进一步了解了小分子调节淀粉样蛋白形成的机理。这篇综述着重介绍了该领域的最新进展,IMS-MS仪器的商业可用性加速了这些进展。本文是《特刊:结构生物学中的质谱》特刊的一部分。

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