- Abstract:
-
Protein amyloid fibrils are a form of linear protein aggregates that are implicated in many neurodegenerative diseases. Here, we study the dynamics of amyloid fibril elongation by performing Langevin dynamic simulations on a coarse-grained model of peptides. Our simulation results suggest that the elongation process is dominated by a series of local minimum due to frustration in monomer-fibril interactions. This rugged energy landscape picture indicates that the amount of recycling of monomer...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1103/physreve.80.041906
-
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- Journal:
- Physical review. E, Statistical, nonlinear, and soft matter physics
- Volume:
- 80
- Issue:
- 4 Pt 1
- Pages:
- 041906
- Publication date:
- 2009-10-05
- DOI:
- EISSN:
-
1550-2376
- ISSN:
-
1539-3755
- URN:
-
uuid:bb0eec3e-ce66-40e5-b06d-90d6638ed19b
- Source identifiers:
-
11948
- Local pid:
- pubs:11948
- Copyright date:
- 2009
Journal article
Elongation dynamics of amyloid fibrils: a rugged energy landscape picture.
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