Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain. [electronic resource]
Producer: 20000616Description: 4250-8 p. digitalISSN:- 0006-2960
- Amino Acid Sequence
- Chaperonin 60 -- chemistry
- Chromatography, Gel
- Deuterium -- metabolism
- Deuterium Oxide -- metabolism
- Escherichia coli
- Guanidine -- pharmacology
- Kinetics
- Light
- Mass Spectrometry
- Models, Molecular
- Molecular Sequence Data
- Molecular Weight
- Pepsin A -- metabolism
- Peptide Fragments -- chemistry
- Protein Denaturation -- drug effects
- Protein Folding
- Protein Structure, Quaternary -- drug effects
- Protein Structure, Tertiary -- drug effects
- Scattering, Radiation
- Thermodynamics
- Urea -- pharmacology
No physical items for this record
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
There are no comments on this title.
Log in to your account to post a comment.