Cargando…
Single molecule mass photometry reveals the dynamic oligomerization of human and plant peroxiredoxins
Protein oligomerization is central to biological function and regulation, yet its experimental quantification and measurement of dynamic transitions in solution remain challenging. Here, we show that single molecule mass photometry quantifies affinity and polydispersity of heterogeneous protein comp...
Autores principales: | Liebthal, Michael, Kushwah, Manish Singh, Kukura, Philipp, Dietz, Karl-Josef |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8571717/ https://www.ncbi.nlm.nih.gov/pubmed/34765909 http://dx.doi.org/10.1016/j.isci.2021.103258 |
Ejemplares similares
-
Peroxiredoxins and Redox Signaling in Plants
por: Liebthal, Michael, et al.
Publicado: (2018) -
Mass photometry enables label-free tracking and mass measurement of single proteins on lipid bilayers
por: Foley, Eric D. B., et al.
Publicado: (2021) -
Single molecule mass photometry of nucleic acids
por: Li, Yiwen, et al.
Publicado: (2020) -
Quantifying the Monomer–Dimer Equilibrium of Tubulin with Mass Photometry
por: Fineberg, Adam, et al.
Publicado: (2020) -
Redox Conformation-Specific Protein–Protein Interactions of the 2-Cysteine Peroxiredoxin in Arabidopsis
por: Liebthal, Michael, et al.
Publicado: (2020)