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Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR
Elucidation of structural changes involved in protein misfolding and amyloid formation is crucial for unraveling the molecular basis of amyloid formation. Here we report structural analyses of the amyloidogenic intermediate and insoluble aggregates of transthyretin (TTR) using solution and solid-sta...
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| Foilsithe in: | Biochemistry |
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| Main Authors: | , , , , , |
| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
2016
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| Ábhair: | |
| Rochtain Ar Líne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4904294/ https://ncbi.nlm.nih.gov/pubmed/26998642 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.6b00164 |
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