Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron–Electron Resonance

[Image: see text] Hsp90 is an important molecular chaperone that facilitates the maturation of client proteins. It is a homodimer, and its function depends on a conformational cycle controlled by ATP hydrolysis and co-chaperones binding. We explored the binding of co-chaperone Sba1 to yeast Hsp90 (y...

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Detalles Bibliográficos
Autores principales: Giannoulis, Angeliki, Feintuch, Akiva, Unger, Tamar, Amir, Shiran, Goldfarb, Daniella
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2021
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8724802/
https://www.ncbi.nlm.nih.gov/pubmed/34928609
http://dx.doi.org/10.1021/acs.jpclett.1c03641

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8724802/
https://www.ncbi.nlm.nih.gov/pubmed/34928609
http://dx.doi.org/10.1021/acs.jpclett.1c03641

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