Conformations and Assembly of Amyloid Oligomers by Electrospray Ionisation - Ion Mobility Spectrometry - Mass Spectrometry

ILLES-TOTH, Eva and SMITH, David (2013). Conformations and Assembly of Amyloid Oligomers by Electrospray Ionisation - Ion Mobility Spectrometry - Mass Spectrometry. Current Analytical Chemistry, 9 (2), 165-180.

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Official URL: http://dx.doi.org/10.2174/157341113805218992
Link to published version:: 10.2174/157341113805218992

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.

Item Type: Article
Research Institute, Centre or Group: Biomolecular Sciences Research Centre
Identification Number: 10.2174/157341113805218992
Depositing User: Marguerite Lyons
Date Deposited: 11 Dec 2013 11:32
Last Modified: 11 Dec 2013 11:32
URI: http://shura.shu.ac.uk/id/eprint/7498

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