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Using chirality to probe the conformational dynamics and assembly of intrinsically disordered amyloid proteins
Intrinsically disordered protein (IDP) conformers occupy large regions of conformational space and display relatively flat energy surfaces. Amyloid-forming IDPs, unlike natively folded proteins, have folding trajectories that frequently involve movements up shallow energy gradients prior to the “dow...
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| Publicado en: | Sci Rep |
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| Autores principales: | , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
Nature Publishing Group UK
2017
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5624888/ https://ncbi.nlm.nih.gov/pubmed/28970487 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-017-10525-5 |
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