Article
Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins.
The Journal of biological chemistry - 11 Nov 1994
Gordon C L, Sather S K, Casjens S, King J
Abstract excerpt
The in vivo conformational substrates of the GroE chaperonins have been difficult to identify, in part because of limited information on in vivo polypeptide chain folding pathways. Temperature-sensitive folding (tsf) mutants have been characterized for the coat protein and tailspike protein of ph...
Topics
- Bacteriophage P22
- Capsid
- Chaperonin 10
- Chaperonin 60
- Escherichia coli Proteins
- Genotype
- Glycoside Hydrolases
- HSP70 Heat-Shock Proteins
- Mutagenesis
- Point Mutation
- Protein Binding
- Protein Conformation
- Protein Denaturation
- Protein Folding
- Salmonella typhimurium
- Thermodynamics
- Viral Proteins
- Viral Tail Proteins