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Stoichiometry and Affinity of Thioflavin T Binding to Sup35p Amyloid Fibrils
In this work two modes of binding of the fluorescent probe thioflavin T to yeast prion protein Sup35p amyloid fibrils were revealed by absorption spectrometry of solutions prepared by equilibrium microdialysis. These binding modes exhibited significant differences in binding affinity and stoichiomet...
Tallennettuna:
| Julkaisussa: | PLoS One |
|---|---|
| Päätekijät: | , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
Public Library of Science
2016
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4882037/ https://ncbi.nlm.nih.gov/pubmed/27228180 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0156314 |
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