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Monitoring site-specific conformational changes in real-time reveals a misfolding mechanism of the prion protein
During pathological aggregation, proteins undergo remarkable conformational re-arrangements to anomalously assemble into a heterogeneous collection of misfolded multimers, ranging from soluble oligomers to insoluble amyloid fibrils. Inspired by fluorescence resonance energy transfer (FRET) measureme...
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| Publicat a: | eLife |
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| Autors principals: | , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
eLife Sciences Publications, Ltd
2019
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6590988/ https://ncbi.nlm.nih.gov/pubmed/31232689 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.44698 |
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