Thermophoretic trap for single amyloid fibril and protein aggregation studies
| العنوان: | Thermophoretic trap for single amyloid fibril and protein aggregation studies |
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| المؤلفون: | Michael Mertig, Daniel Huster, Martin Fränzl, Tobias Thalheim, Frank Cichos, Juliane Posseckardt, Juliane Adler |
| المصدر: | Nature Methods. 16:611-614 |
| بيانات النشر: | Springer Science and Business Media LLC, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | Amyloid, Protein Folding, 0303 health sciences, Chemistry, Nucleation, Rotational diffusion, macromolecular substances, Cell Biology, Protein aggregation, Fibril, Amyloid fibril, Biochemistry, Diffusion, Protein Aggregates, 03 medical and health sciences, mental disorders, Biophysics, Protein folding, Molecular Biology, 030304 developmental biology, Biotechnology |
| الوصف: | The study of the aggregation of soluble proteins into highly ordered, insoluble amyloid fibrils is fundamental for the understanding of neurodegenerative disorders. Here, we present a method for the observation of single amyloid fibrils that allows the investigation of fibril growth, secondary nucleation or fibril breakup that is typically hidden in the average ensemble. Our approach of thermophoretic trapping and rotational diffusion measurements is demonstrated for single Aβ40, Aβ42 and pyroglutamyl-modified amyloid-β variant (pGlu3-Aβ3-40) amyloid fibrils. |
| تدمد: | 1548-7105 1548-7091 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19ab92ae9a16dd5ca22333d586930aa9 https://doi.org/10.1038/s41592-019-0451-6 |
| حقوق: | CLOSED |
| رقم الأكسشن: | edsair.doi.dedup.....19ab92ae9a16dd5ca22333d586930aa9 |
| قاعدة البيانات: | OpenAIRE |
Find this article in full text from Springer Verlag. | تدمد: | 15487105 15487091 |
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