Influence of the GroE molecular chaperone machine on the in vitro refolding ofEscherichia coliβ-galactosidase
Author:
Funder
NSF award
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560050309/fullpdf
Reference46 articles.
1. Binding of a chaperonin to the folding intermediates of lactate dehydrogenase;Badcoe;Biochemistry,1991
2. Chaperonins and protein folding;Baneyx;Ann New York Acad Sci,1994
3. A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides;Baneyx;J Biol Chem,1992
4. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å;Braig;Nature,1994
5. A polypeptide bound by the chaperonin GroEL is localized within a central cavity;Braig;Proc Natl Acad Sci USA,1993
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