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Chaperonins: Nanocarriers with Biotechnological Applications

Chaperonins are molecular chaperones found in all kingdoms of life, and as such they assist in the folding of other proteins. Structurally, chaperonins are cylinders composed of two back-to-back rings, each of which is an oligomer of ~60-kDa proteins. Chaperonins are found in two main conformations,...

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Detalles Bibliográficos
Autores principales: Pipaón, Sergio, Gragera, Marcos, Bueno-Carrasco, M. Teresa, García-Bernalt Diego, Juan, Cantero, Miguel, Cuéllar, Jorge, Fernández-Fernández, María Rosario, Valpuesta, José María
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7922521/
https://www.ncbi.nlm.nih.gov/pubmed/33671209
http://dx.doi.org/10.3390/nano11020503
Descripción
Sumario:Chaperonins are molecular chaperones found in all kingdoms of life, and as such they assist in the folding of other proteins. Structurally, chaperonins are cylinders composed of two back-to-back rings, each of which is an oligomer of ~60-kDa proteins. Chaperonins are found in two main conformations, one in which the cavity is open and ready to recognise and trap unfolded client proteins, and a “closed” form in which folding takes place. The conspicuous properties of this structure (a cylinder containing a cavity that allows confinement) and the potential to control its closure and aperture have inspired a number of nanotechnological applications that will be described in this review.