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: Pipaón, Sergio, Gragera, Marcos, Bueno-Carrasco, M. Teresa, García-Bernalt Diego, Juan, Cantero, Miguel, Cuéllar, Jorge, Fernández-Fernández, María Rosario, Valpuesta, José M.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/376160
Acceso en línea:http://hdl.handle.net/10261/376160
Access Level:acceso abierto
Palabra clave:Molecular chaperones
Chaperonins
Nanocarriers
Nanoreactors
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.