Cargando…
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...
Autores principales: | Sulatskaya, Anna I., Kuznetsova, Irina M., Belousov, Mikhail V., Bondarev, Stanislav A., Zhouravleva, Galina A., Turoverov, Konstantin K. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4882037/ https://www.ncbi.nlm.nih.gov/pubmed/27228180 http://dx.doi.org/10.1371/journal.pone.0156314 |
Ejemplares similares
-
Analyzing Thioflavin T Binding to Amyloid Fibrils by an Equilibrium Microdialysis-Based Technique
por: Kuznetsova, Irina M., et al.
Publicado: (2012) -
Fluorescence Quantum Yield of Thioflavin T in Rigid Isotropic Solution and Incorporated into the Amyloid Fibrils
por: Sulatskaya, Anna I., et al.
Publicado: (2010) -
Thioflavin T fluoresces as excimer in highly concentrated aqueous solutions and as monomer being incorporated in amyloid fibrils
por: Sulatskaya, Anna I., et al.
Publicado: (2017) -
Investigation of α-Synuclein Amyloid Fibrils Using the Fluorescent Probe Thioflavin T
por: Sulatskaya, Anna I., et al.
Publicado: (2018) -
M60-like metalloprotease domain of the Escherichia coli YghJ protein forms amyloid fibrils
por: Belousov, Mikhail V., et al.
Publicado: (2018)