Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference35 articles.
1. Protein folding in the cell: competing models of chaperonin function
2. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
3. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
4. Residues in chaperonin GroEL required for polypeptide binding and release
5. Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy
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