Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(94)80381-1/fullpdf
Reference28 articles.
1. Protein folding in the cell
2. Purification and properties of groE, a host protein involved in bacteriophage assembly
3. Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly
4. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.
5. A polypeptide bound by the chaperonin groEL is localized within a central cavity.
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