Abstract
We 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
Original language | English |
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Pages (from-to) | 1 - 5 |
Number of pages | 5 |
Journal | Nanotechnology |
Volume | 18 |
Issue number | 4 (044031) |
Publication status | Published - 2007 |
Externally published | Yes |