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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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Bibliografski detalji
Izdano u:eLife
Glavni autori: Sengupta, Ishita, Udgaonkar, Jayant
Format: Artigo
Jezik:Inglês
Izdano: eLife Sciences Publications, Ltd 2019
Teme:
Online pristup: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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