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Pathogenic Mutations Induce Partial Structural Changes in Native β-Sheet Structure of Transthyretin and Accelerate Aggregation
Amyloid formation of natively folded proteins involves global and/or local unfolding of the native state to form aggregation-prone intermediates. Here we report solid-state NMR structural studies of amyloid derived from wild-type (WT) and more aggressive mutant forms of transthyretin (TTR) to invest...
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| Publicado no: | Biochemistry |
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| Main Authors: | , , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2017
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5745580/ https://ncbi.nlm.nih.gov/pubmed/28820582 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.7b00658 |
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