๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Specificity in chaperonin-mediated protein folding

โœ Scribed by Tian, Guoling; Vainberg, Irina E.; Tap, William D.; Lewis, Sally A.; Cowan, Nicholas J.

Book ID
109792035
Publisher
Nature Publishing Group
Year
1995
Tongue
English
Weight
477 KB
Volume
375
Category
Article
ISSN
0028-0836

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๐Ÿ“œ SIMILAR VOLUMES

A simple model of chaperonin-mediated pr
A simple model of chaperonin-mediated protein folding
โœ Chan, Hue Sun; Dill, Ken A. ๐Ÿ“‚ Article ๐Ÿ“… 1996 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 678 KB

Chaperonins are oligomeric proteins that help other proteins fold. They act, according to the "Anfinsen cage" or "box of infinite dilution" model, to provide private space, protected from aggregation, where a protein can fold. Recent evidence indicates, however, that proteins are often ejected from

The chaperonin cycle and protein folding
The chaperonin cycle and protein folding
โœ Peter Lund ๐Ÿ“‚ Article ๐Ÿ“… 1994 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 676 KB

The process of protein folding in the cell is now known to depend on the action of other proteins. These proteins include molecular chaperones, which interact non-covalently with proteins as they fold and improve the final yields of active protein in the cell. The precise mechanism by which molecula