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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...
| Autores principales: | , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
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eLife Sciences Publications, Ltd
2019
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6590988/ https://www.ncbi.nlm.nih.gov/pubmed/31232689 http://dx.doi.org/10.7554/eLife.44698 |