A Monomeric Variant of GroEL Binds Nucleotides but Is Inactive as a Molecular Chaperone
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference42 articles.
1. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.
2. ATP induces large quaternary rearrangements in a cage-like chaperonin structure
3. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
4. A polypeptide bound by the chaperonin groEL is localized within a central cavity.
5. Residues in chaperonin GroEL required for polypeptide binding and release
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