The Molecular Chaperonin cpn60 Displays Local Flexibility That Is Reduced after Binding with an Unfolded Protein
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference45 articles.
1. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
2. Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese
3. GroEL, GroES, and ATP-dependent folding and spontaneous assembly of ornithine transcarbamylase.
4. GroE dependence of refolding and holoenzyme formation of 6-hydroxy-D-nicotine oxidase.
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