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Chaperonins: Nanocarriers with Biotechnological Applications.

Sergio PipaónMarcos GrageraM Teresa Bueno-CarrascoJuan García-Bernalt DiegoMiguel CanteroJorge CuéllarMaría Rosario Fernández-FernándezJosé María Valpuesta
Published in: Nanomaterials (Basel, Switzerland) (2021)
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.
Keyphrases
  • single molecule
  • molecular dynamics simulations
  • minimally invasive
  • endoplasmic reticulum stress
  • oxidative stress