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.
Full text not available from this repository.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 |
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Research Institute, Centre or Group - Does NOT include content added after October 2018: | Biomedical Research Centre |
Identification Number: | https://doi.org/10.2174/157341113805218992 |
Page Range: | 165-180 |
Depositing User: | Users 3084 not found. |
Date Deposited: | 11 Dec 2013 11:32 |
Last Modified: | 18 Mar 2021 19:30 |
URI: | https://shura.shu.ac.uk/id/eprint/7498 |
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