Source:http://linkedlifedata.com/resource/pubmed/id/21280130
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2011-1-31
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| pubmed:abstractText |
The major component of neural inclusions that are the pathological hallmark of Parkinson's disease are amyloid fibrils of the protein ?-synuclein (aS). Here we investigated if the disease-related mutation A30P not only modulates the kinetics of aS aggregation, but also alters the structure of amyloid fibrils. To this end we optimized the method of quenched hydrogen/deuterium exchange coupled to NMR spectroscopy and performed two-dimensional proton-detected high-resolution magic angle spinning experiments. The combined data indicate that the A30P mutation does not cause changes in the number, location and overall arrangement of ?-strands in amyloid fibrils of aS. At the same time, several residues within the fibrillar core retain nano-second dynamics. We conclude that the increased pathogenicity related to the familial A30P mutation is unlikely to be caused by a mutation-induced change in the conformation of aS aggregates.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
1469-896X
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright © 2010 The Protein Society.
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| pubmed:issnType |
Electronic
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| pubmed:volume |
20
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
387-95
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| pubmed:meshHeading | |
| pubmed:year |
2011
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| pubmed:articleTitle |
Conserved core of amyloid fibrils of wild type and A30P mutant ?-synuclein.
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| pubmed:affiliation |
Department for NMR based Structural Biology, Max Planck Institute for Biophysical Chemistry, D-37077, Goettingen, Germany.
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| pubmed:publicationType |
Journal Article
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