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  Determination of amyloid core structure using chemical shifts.

Skora, L., & Zweckstetter, M. (2012). Determination of amyloid core structure using chemical shifts. Protein Science, 21(12), 1948-1953. doi:10.1002/pro.2170.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-6FE4-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-2F10-0
Genre: Journal Article

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1587230.pdf (Publisher version), 232KB
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 Creators:
Skora, L.1, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Free keywords: Fibril; NMR; structure; prion
 Abstract: Amyloid fibrils are the pathological hallmark of a large variety of neurodegenerative disorders. The structural characterization of amyloid fibrils, however, is challenging due to their non-crystalline, heterogeneous, and often dynamic nature. Thus, the structure of amyloid fibrils of many proteins is still unknown. We here show that the structure calculation program CS-Rosetta can be used to obtain insight into the core structure of amyloid fibrils. Driven by experimental solid-state NMR chemical shifts and taking into account the polymeric nature of fibrils CS-Rosetta allows modeling of the core of amyloid fibrils. Application to the Y145X stop mutant of the human prion protein reveals a left-handed beta-helix.

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Language(s): eng - English
 Dates: 2012-10-022012-12
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/pro.2170
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Title: Protein Science
Source Genre: Journal
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Pages: - Volume / Issue: 21 (12) Sequence Number: - Start / End Page: 1948 - 1953 Identifier: -