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Elongation dynamics of amyloid fibrils: a rugged energy landscape picture.

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...

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Publication status:
Published

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Publisher copy:
10.1103/physreve.80.041906

Authors


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

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