Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsb1295-1083.pdf
Reference41 articles.
1. Principles that Govern the Folding of Protein Chains
2. Proteins as molecular chaperones
3. Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
4. Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1
5. A polypeptide bound by the chaperonin groEL is localized within a central cavity.
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