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Conformational dynamics of the Hsp70 chaperone throughout key steps of its ATPase cycle
The 70 kDa heat shock proteins (Hsp70s) are highly versatile molecular chaperones that assist in a wide variety of protein-folding processes. They exert their functions by continuously cycling between states of low and high affinity for client polypeptides, driven by ATP-binding and hydrolysis. This...
| Autores principales: | , , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
| Publicado: |
National Academy of Sciences
2022
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9889847/ https://www.ncbi.nlm.nih.gov/pubmed/36409905 http://dx.doi.org/10.1073/pnas.2123238119 |