Tuomas P J Knowles et al 2007 Nanotechnology 18 044031 doi:10.1088/0957-4484/18/4/044031
Tuomas P J Knowles1,2, Jeffrey F Smith1,2, Glyn L Devlin3, Christopher M Dobson2,3 and Mark E Welland1
Show affiliationsWe discuss the application of atomic force microscopy to characterize supra-molecular ordering in elongated protein aggregates such as amyloid fibrils. The measurements reveal that the one-dimensional defect density along these structures is comparable to that found in true three-dimensional macromolecular crystals. The high level of structural order has important implications for understanding the nature of the interactions responsible for protein aggregation, and sheds light on the involvement of amyloid fibrils in aberrant biological pathways.
87.15.B- Structure of biomolecules
87.15.K- Molecular interactions; membrane-protein interactions
Issue 4 (31 January 2007)
Received 25 September 2006, in final form 6 November 2006
Published 21 December 2006
Tuomas P J Knowles et al 2007 Nanotechnology 18 044031
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