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2000
Volume 9, Issue 2
  • ISSN: 1573-4110
  • E-ISSN: 1875-6727

Abstract

Amyloid structures accumulate and propagate through self-assembly of partially folded proteins and peptides, resulting in a range of disease states. Key to understanding amyloid disease is the characterisation of the often toxic oligomeric species formed during the early stages of fibril assembly. Electrospray ionisation- ion mobility spectrometry - mass spectrometry (ESI-IMS-MS) has emerged as a powerful tool to investigate amyloid oligomer assembly and protein conformation change. In this review we focus on the role of ESI-IMS-MS in understanding and probing conformational changes and the early stages of protein aggregation.

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/content/journals/cac/10.2174/157341113805218992
2013-04-01
2025-05-03
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