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In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution

Protein folding is often hampered by intermolecular protein aggregation, which can be prevented by a variety of chaperones in the cell. Bacterial chaperonin GroEL is a ring-shaped chaperone that forms complexes with its cochaperonin GroES, creating central cavities to accommodate client proteins (al...

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Detalles Bibliográficos
Autores principales: Taguchi, Hideki, Koike-Takeshita, Ayumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9950496/
https://www.ncbi.nlm.nih.gov/pubmed/36845542
http://dx.doi.org/10.3389/fmolb.2023.1091677