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Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR

The 140-residue protein α-synuclein (AS) is able to form amyloid fibrils and as such is the main component of protein inclusions involved in Parkinson's disease. We have investigated the structure and dynamics of full-length AS fibrils by high-resolution solid-state NMR spectroscopy. Homonuclea...

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Bibliografiske detaljer
Main Authors: Heise, Henrike, Hoyer, Wolfgang, Becker, Stefan, Andronesi, Ovidiu C., Riedel, Dietmar, Baldus, Marc
Format: Artigo
Sprog:Inglês
Udgivet: National Academy of Sciences 2005
Fag:
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1276071/
https://ncbi.nlm.nih.gov/pubmed/16247008
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0506109102
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