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Amyloid-like Fibrils from a Domain-swapping Protein Feature a Parallel, in-Register Conformation without Native-like Interactions

The formation of amyloid-like fibrils is characteristic of various diseases, but the underlying mechanism and the factors that determine whether, when, and how proteins form amyloid, remain uncertain. Certain mechanisms have been proposed based on the three-dimensional or runaway domain swapping, in...

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Bibliographic Details
Main Authors: Li, Jun, Hoop, Cody L., Kodali, Ravindra, Sivanandam, V. N., van der Wel, Patrick C. A.
Format: Artigo
Language:Inglês
Published: American Society for Biochemistry and Molecular Biology 2011
Subjects:
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC3190706/
https://ncbi.nlm.nih.gov/pubmed/21715337
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.261750
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