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.
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.
|Research Institute, Centre or Group:||Biomolecular Sciences Research Centre|
|Depositing User:||Marguerite Lyons|
|Date Deposited:||11 Dec 2013 11:32|
|Last Modified:||11 Dec 2013 11:32|
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